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Copper in PDB 2iwk: Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution

Enzymatic activity of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution

All present enzymatic activity of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution:
1.7.99.6;

Protein crystallography data

The structure of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution, PDB code: 2iwk was solved by K.Paraskevopoulos, S.V.Antonyuk, R.G.Sawers, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.7
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.114, 120.913, 137.343, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.7

Other elements in 2iwk:

The structure of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution also contains other interesting chemical elements:

Iodine (I) 15 atoms
Chlorine (Cl) 8 atoms
Calcium (Ca) 28 atoms
Sodium (Na) 30 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution (pdb code 2iwk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 12 binding sites of Copper where determined in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution, PDB code: 2iwk:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12;

Copper binding site 1 out of 12 in 2iwk

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Copper binding site 1 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1598

b:23.4
occ:1.00
ND1 A:HIS543 2.2 24.3 1.0
SG A:CYS582 2.3 19.6 1.0
SG A:CYS578 2.4 20.0 1.0
CU A:CU1599 2.5 26.3 1.0
SD A:MET589 2.6 21.5 1.0
CE1 A:HIS543 3.1 23.0 1.0
CB A:CYS578 3.2 19.9 1.0
CE A:MET589 3.2 24.0 1.0
CB A:CYS582 3.3 21.1 1.0
CG A:HIS543 3.3 20.4 1.0
CB A:HIS543 3.7 19.1 1.0
O A:TRP580 3.8 20.8 1.0
CG A:MET589 3.9 18.3 1.0
CA A:HIS543 4.1 18.7 1.0
NE2 A:HIS543 4.3 21.1 1.0
CD2 A:HIS543 4.4 20.5 1.0
ND1 A:HIS586 4.4 22.4 1.0
CB A:MET589 4.5 18.0 1.0
CA A:CYS578 4.6 19.2 1.0
CA A:CYS582 4.7 20.2 1.0
O A:THR542 4.7 18.5 1.0
N A:GLY544 4.9 18.5 1.0
N A:CYS582 4.9 20.9 1.0
C A:TRP580 4.9 22.0 1.0

Copper binding site 2 out of 12 in 2iwk

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Copper binding site 2 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1599

b:26.3
occ:1.00
ND1 A:HIS586 2.0 22.4 1.0
SG A:CYS582 2.4 19.6 1.0
CU A:CU1598 2.5 23.4 1.0
O A:TRP580 2.5 20.8 1.0
SG A:CYS578 2.5 20.0 1.0
CE1 A:HIS586 2.8 22.8 1.0
CG A:HIS586 3.1 20.9 1.0
CB A:CYS582 3.3 21.1 1.0
CB A:CYS578 3.4 19.9 1.0
C A:TRP580 3.4 22.0 1.0
N A:CYS582 3.4 20.9 1.0
CB A:HIS586 3.6 21.1 1.0
CA A:HIS586 4.0 20.3 1.0
CA A:PHE581 4.0 22.6 1.0
CA A:CYS582 4.0 20.2 1.0
NE2 A:HIS586 4.0 23.8 1.0
C A:PHE581 4.1 22.4 1.0
N A:PHE581 4.1 23.1 1.0
SD A:MET589 4.2 21.5 1.0
CD2 A:HIS586 4.2 23.6 1.0
O A:CYS578 4.2 21.0 1.0
O A:HIS586 4.4 18.9 1.0
C A:CYS578 4.4 19.7 1.0
N A:TRP580 4.4 20.5 1.0
ND1 A:HIS543 4.5 24.3 1.0
CA A:TRP580 4.5 21.6 1.0
CA A:CYS578 4.6 19.2 1.0
C A:HIS586 4.6 20.7 1.0
CB A:MET589 4.7 18.0 1.0
CG A:MET589 4.9 18.3 1.0
C A:CYS582 4.9 20.1 1.0

Copper binding site 3 out of 12 in 2iwk

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Copper binding site 3 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1600

b:37.2
occ:0.40
CU1 A:CUZ1600 0.0 37.2 0.4
S1 A:CUZ1600 1.9 34.6 0.4
NE2 A:HIS391 2.0 23.2 1.0
CU4 A:CUZ1600 2.6 34.5 0.4
NE2 A:HIS94 2.6 34.8 1.0
CU3 A:CUZ1600 2.7 33.2 0.4
CE1 A:HIS391 2.8 26.6 1.0
CD2 A:HIS391 3.2 26.4 1.0
CE1 A:HIS94 3.5 34.4 1.0
CD2 A:HIS94 3.5 33.3 1.0
CU2 A:CUZ1600 3.5 30.9 0.4
ND2 A:ASN204 3.7 26.0 1.0
NE2 A:HIS142 3.8 36.1 1.0
ND1 A:HIS391 4.0 24.1 1.0
CB A:HIS452 4.2 25.0 1.0
CE1 A:HIS340 4.2 23.6 1.0
CG A:HIS391 4.2 23.6 1.0
CE1 A:HIS142 4.3 37.0 1.0
ND1 A:HIS452 4.4 32.5 1.0
NE2 A:HIS340 4.4 22.6 1.0
OD1 A:ASN204 4.5 29.6 1.0
CG A:ASN204 4.6 28.5 1.0
ND1 A:HIS94 4.6 34.5 1.0
ND1 A:HIS93 4.6 36.7 1.0
I A:IOD1605 4.6 35.2 0.4
CB A:HIS93 4.6 24.3 1.0
CG A:HIS94 4.6 29.1 1.0
CG A:HIS452 4.7 25.2 1.0
CD2 A:HIS142 4.7 35.4 1.0
NE2 A:HIS285 4.8 29.4 1.0
O A:HIS93 4.9 22.2 1.0

Copper binding site 4 out of 12 in 2iwk

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Copper binding site 4 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1600

b:30.9
occ:0.40
CU2 A:CUZ1600 0.0 30.9 0.4
NE2 A:HIS340 2.0 22.6 1.0
NE2 A:HIS285 2.1 29.4 1.0
I A:IOD1605 2.4 35.2 0.4
S1 A:CUZ1600 2.6 34.6 0.4
CE1 A:HIS340 2.8 23.6 1.0
CD2 A:HIS285 3.0 27.7 1.0
CE1 A:HIS285 3.2 31.1 1.0
CD2 A:HIS340 3.2 26.1 1.0
CU3 A:CUZ1600 3.2 33.2 0.4
NE2 A:HIS391 3.4 23.2 1.0
CU1 A:CUZ1600 3.5 37.2 0.4
CD2 A:HIS391 3.8 26.4 1.0
ND1 A:HIS340 4.0 21.6 1.0
CE1 A:HIS391 4.1 26.6 1.0
CG A:HIS285 4.2 26.6 1.0
CG A:HIS340 4.2 22.5 1.0
ND1 A:HIS285 4.2 29.3 1.0
OD1 A:ASN204 4.4 29.6 1.0
CG A:HIS391 4.5 23.6 1.0
CU4 A:CUZ1600 4.6 34.5 0.4
ND1 A:HIS391 4.7 24.1 1.0
CE2 B:PHE581 4.8 28.4 1.0

Copper binding site 5 out of 12 in 2iwk

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Copper binding site 5 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1600

b:33.2
occ:0.40
CU3 A:CUZ1600 0.0 33.2 0.4
ND1 A:HIS452 2.3 32.5 1.0
CU4 A:CUZ1600 2.3 34.5 0.4
S1 A:CUZ1600 2.4 34.6 0.4
CU1 A:CUZ1600 2.7 37.2 0.4
I A:IOD1605 2.9 35.2 0.4
CU2 A:CUZ1600 3.2 30.9 0.4
CG A:HIS452 3.3 25.2 1.0
CE1 A:HIS452 3.3 35.1 1.0
NE2 A:HIS391 3.4 23.2 1.0
CB A:HIS452 3.5 25.0 1.0
O B:HOH2413 3.6 50.4 1.0
CD2 A:HIS391 3.7 26.4 1.0
ND1 A:HIS93 4.0 36.7 1.0
NE2 A:HIS142 4.3 36.1 1.0
NE2 A:HIS452 4.4 31.1 1.0
CD2 A:HIS452 4.4 29.4 1.0
CA A:HIS452 4.5 24.7 1.0
CE1 A:HIS391 4.6 26.6 1.0
NZ A:LYS412 4.7 30.9 1.0
NE2 A:HIS285 4.7 29.4 1.0
CE2 B:PHE581 4.7 28.4 1.0
CE1 A:HIS93 4.7 36.2 1.0
CD2 B:PHE581 4.8 29.4 1.0
NE2 A:HIS340 4.9 22.6 1.0
CG A:HIS93 5.0 28.8 1.0
CG A:HIS391 5.0 23.6 1.0

Copper binding site 6 out of 12 in 2iwk

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Copper binding site 6 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1600

b:34.5
occ:0.40
CU4 A:CUZ1600 0.0 34.5 0.4
NE2 A:HIS142 2.2 36.1 1.0
S1 A:CUZ1600 2.3 34.6 0.4
CU3 A:CUZ1600 2.3 33.2 0.4
ND1 A:HIS93 2.4 36.7 1.0
CU1 A:CUZ1600 2.6 37.2 0.4
CD2 A:HIS142 3.0 35.4 1.0
CE1 A:HIS93 3.3 36.2 1.0
ND1 A:HIS452 3.4 32.5 1.0
CE1 A:HIS142 3.4 37.0 1.0
CG A:HIS93 3.4 28.8 1.0
O B:HOH2413 3.5 50.4 1.0
CB A:HIS93 3.7 24.3 1.0
CE1 A:HIS452 3.9 35.1 1.0
NE2 A:HIS94 3.9 34.8 1.0
CE1 A:HIS94 4.0 34.4 1.0
CG A:HIS452 4.1 25.2 1.0
CG A:HIS142 4.2 31.5 1.0
ND1 A:HIS142 4.4 35.2 1.0
CB A:HIS452 4.4 25.0 1.0
NE2 A:HIS391 4.4 23.2 1.0
NE2 A:HIS93 4.4 34.1 1.0
CD2 A:HIS93 4.5 34.5 1.0
CU2 A:CUZ1600 4.6 30.9 0.4
NE2 A:HIS452 4.8 31.1 1.0
CD2 A:HIS452 4.9 29.4 1.0
CA A:HIS93 5.0 23.0 1.0
CD2 A:HIS94 5.0 33.3 1.0
ND1 A:HIS94 5.0 34.5 1.0

Copper binding site 7 out of 12 in 2iwk

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Copper binding site 7 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1598

b:26.8
occ:1.00
ND1 B:HIS543 2.3 21.2 1.0
SG B:CYS578 2.3 21.4 1.0
CU B:CU1599 2.5 28.9 1.0
SG B:CYS582 2.5 23.9 1.0
SD B:MET589 2.5 23.2 1.0
CE1 B:HIS543 3.1 19.8 1.0
CB B:CYS578 3.2 19.8 1.0
CE B:MET589 3.3 24.3 1.0
CB B:CYS582 3.3 25.1 1.0
CG B:HIS543 3.4 20.2 1.0
O B:TRP580 3.8 22.5 1.0
CB B:HIS543 3.8 21.8 1.0
CG B:MET589 3.9 22.1 1.0
CA B:HIS543 4.1 21.1 1.0
NE2 B:HIS543 4.3 22.0 1.0
CB B:MET589 4.4 22.8 1.0
CD2 B:HIS543 4.4 20.6 1.0
ND1 B:HIS586 4.5 24.8 1.0
CA B:CYS578 4.6 18.9 1.0
CA B:CYS582 4.7 25.2 1.0
O B:THR542 4.8 22.8 1.0
N B:GLY544 4.8 20.6 1.0
C B:TRP580 4.9 22.5 1.0
N B:CYS582 4.9 26.1 1.0

Copper binding site 8 out of 12 in 2iwk

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Copper binding site 8 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1599

b:28.9
occ:1.00
ND1 B:HIS586 2.1 24.8 1.0
SG B:CYS582 2.3 23.9 1.0
O B:TRP580 2.5 22.5 1.0
CU B:CU1598 2.5 26.8 1.0
SG B:CYS578 2.6 21.4 1.0
CE1 B:HIS586 3.0 22.9 1.0
CB B:CYS582 3.2 25.1 1.0
CG B:HIS586 3.2 24.6 1.0
N B:CYS582 3.4 26.1 1.0
C B:TRP580 3.5 22.5 1.0
CB B:CYS578 3.6 19.8 1.0
CB B:HIS586 3.7 25.1 1.0
CA B:CYS582 3.9 25.2 1.0
CA B:PHE581 4.0 24.7 1.0
C B:PHE581 4.0 25.2 1.0
CA B:HIS586 4.1 25.2 1.0
SD B:MET589 4.1 23.2 1.0
N B:PHE581 4.1 24.3 1.0
NE2 B:HIS586 4.2 26.9 1.0
O B:CYS578 4.2 21.0 1.0
CD2 B:HIS586 4.3 25.1 1.0
O B:HIS586 4.4 24.3 1.0
N B:TRP580 4.4 19.6 1.0
CA B:TRP580 4.5 22.2 1.0
ND1 B:HIS543 4.5 21.2 1.0
C B:CYS578 4.5 19.6 1.0
CB B:MET589 4.6 22.8 1.0
CA B:CYS578 4.7 18.9 1.0
C B:HIS586 4.7 25.8 1.0
C B:CYS582 4.8 25.1 1.0
CG B:MET589 4.9 22.1 1.0
N B:HIS583 5.0 24.5 1.0

Copper binding site 9 out of 12 in 2iwk

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Copper binding site 9 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1600

b:29.7
occ:0.50
CU1 B:CUZ1600 0.0 29.7 0.5
S1 B:CUZ1600 2.0 24.5 0.5
NE2 B:HIS391 2.1 27.8 1.0
NE2 B:HIS94 2.4 32.4 1.0
CU4 B:CUZ1600 2.7 27.5 0.5
CU3 B:CUZ1600 2.8 30.6 0.5
CE1 B:HIS391 2.9 28.4 1.0
CD2 B:HIS391 3.2 27.7 1.0
CD2 B:HIS94 3.3 31.9 1.0
CE1 B:HIS94 3.3 33.7 1.0
CU2 B:CUZ1600 3.4 25.2 0.5
NE2 B:HIS142 3.7 31.7 1.0
ND2 B:ASN204 3.9 25.6 1.0
CE1 B:HIS340 4.1 22.8 1.0
ND1 B:HIS391 4.1 25.8 1.0
NE2 B:HIS340 4.1 22.7 1.0
CB B:HIS452 4.2 21.6 1.0
CG B:HIS391 4.3 24.1 1.0
CE1 B:HIS142 4.3 30.6 1.0
CB B:HIS93 4.4 22.4 1.0
ND1 B:HIS452 4.4 26.2 1.0
ND1 B:HIS94 4.4 26.1 1.0
CG B:HIS94 4.4 23.6 1.0
ND1 B:HIS93 4.5 30.1 1.0
OD1 B:ASN204 4.5 29.1 1.0
I B:IOD1605 4.6 28.3 0.5
CG B:ASN204 4.6 26.4 1.0
CD2 B:HIS142 4.7 30.9 1.0
CG B:HIS452 4.7 23.8 1.0
O B:HIS93 4.7 20.5 1.0
NE2 B:HIS285 4.8 23.5 1.0
CG B:HIS93 4.9 26.3 1.0

Copper binding site 10 out of 12 in 2iwk

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Copper binding site 10 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1600

b:25.2
occ:0.50
CU2 B:CUZ1600 0.0 25.2 0.5
NE2 B:HIS340 2.1 22.7 1.0
NE2 B:HIS285 2.1 23.5 1.0
S1 B:CUZ1600 2.4 24.5 0.5
I B:IOD1605 2.5 28.3 0.5
CE1 B:HIS340 3.0 22.8 1.0
CU3 B:CUZ1600 3.0 30.6 0.5
CD2 B:HIS285 3.1 24.8 1.0
CE1 B:HIS285 3.1 23.5 1.0
CD2 B:HIS340 3.2 22.2 1.0
CU1 B:CUZ1600 3.4 29.7 0.5
NE2 B:HIS391 3.5 27.8 1.0
CD2 B:HIS391 3.8 27.7 1.0
ND1 B:HIS340 4.1 22.3 1.0
CE1 B:HIS391 4.2 28.4 1.0
ND1 B:HIS285 4.2 22.9 1.0
CG B:HIS285 4.2 21.0 1.0
CG B:HIS340 4.3 19.3 1.0
OD1 B:ASN204 4.4 29.1 1.0
CU4 B:CUZ1600 4.5 27.5 0.5
CG B:HIS391 4.6 24.1 1.0
ND1 B:HIS391 4.8 25.8 1.0
CE2 A:PHE581 4.8 25.2 1.0

Copper binding site 11 out of 12 in 2iwk

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Copper binding site 11 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 11 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1600

b:30.6
occ:0.50
CU3 B:CUZ1600 0.0 30.6 0.5
S1 B:CUZ1600 2.1 24.5 0.5
ND1 B:HIS452 2.2 26.2 1.0
CU4 B:CUZ1600 2.6 27.5 0.5
I B:IOD1605 2.8 28.3 0.5
CU1 B:CUZ1600 2.8 29.7 0.5
CU2 B:CUZ1600 3.0 25.2 0.5
CE1 B:HIS452 3.1 28.4 1.0
CG B:HIS452 3.2 23.8 1.0
CB B:HIS452 3.6 21.6 1.0
NE2 B:HIS391 3.6 27.8 1.0
CD2 B:HIS391 3.7 27.7 1.0
ND1 B:HIS93 3.9 30.1 1.0
NE2 B:HIS452 4.3 24.6 1.0
NE2 B:HIS142 4.3 31.7 1.0
CD2 B:HIS452 4.3 23.8 1.0
CA B:HIS452 4.5 21.8 1.0
NZ B:LYS412 4.5 28.9 1.0
NE2 B:HIS285 4.6 23.5 1.0
CE2 A:PHE581 4.6 25.2 1.0
CE1 B:HIS93 4.7 31.7 1.0
NE2 B:HIS340 4.7 22.7 1.0
CD2 A:PHE581 4.8 25.6 1.0
CG B:HIS93 4.9 26.3 1.0
CE1 B:HIS391 4.9 28.4 1.0
CE1 B:HIS285 5.0 23.5 1.0
NE2 B:HIS94 5.0 32.4 1.0

Copper binding site 12 out of 12 in 2iwk

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Copper binding site 12 out of 12 in the Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 12 of Inhibitor-Bound Form of Nitrous Oxide Reductase From Achromobacter Cycloclastes at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1600

b:27.5
occ:0.50
CU4 B:CUZ1600 0.0 27.5 0.5
NE2 B:HIS142 2.1 31.7 1.0
S1 B:CUZ1600 2.2 24.5 0.5
ND1 B:HIS93 2.2 30.1 1.0
CU3 B:CUZ1600 2.6 30.6 0.5
CU1 B:CUZ1600 2.7 29.7 0.5
CD2 B:HIS142 2.8 30.9 1.0
CE1 B:HIS93 3.1 31.7 1.0
CG B:HIS93 3.2 26.3 1.0
CE1 B:HIS142 3.3 30.6 1.0
ND1 B:HIS452 3.5 26.2 1.0
CB B:HIS93 3.5 22.4 1.0
NE2 B:HIS94 3.8 32.4 1.0
CE1 B:HIS94 3.8 33.7 1.0
CE1 B:HIS452 4.0 28.4 1.0
CG B:HIS142 4.1 27.8 1.0
CG B:HIS452 4.1 23.8 1.0
ND1 B:HIS142 4.2 30.8 1.0
NE2 B:HIS93 4.3 27.4 1.0
CD2 B:HIS93 4.3 30.2 1.0
CU2 B:CUZ1600 4.5 25.2 0.5
CB B:HIS452 4.5 21.6 1.0
NE2 B:HIS391 4.6 27.8 1.0
NE2 B:HIS452 4.8 24.6 1.0
CD2 B:HIS94 4.8 31.9 1.0
CE A:MET587 4.8 33.0 1.0
ND1 B:HIS94 4.8 26.1 1.0
CA B:HIS93 4.9 21.9 1.0
CD2 B:HIS452 4.9 23.8 1.0

Reference:

K.Paraskevopoulos, S.V.Antonyuk, R.G.Sawers, R.R.Eady, S.S.Hasnain. Insight Into Catalysis of Nitrous Oxide Reductase From High-Resolution Structures of Resting and Inhibitor-Bound Enzyme From Achromobacter Cycloclastes. J.Mol.Biol. V. 362 55 2006.
ISSN: ISSN 0022-2836
PubMed: 16904686
DOI: 10.1016/J.JMB.2006.06.064
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