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Copper in PDB 2aqr: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant

Enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant, PDB code: 2aqr was solved by M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.47 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.840, 65.052, 77.443, 90.00, 121.02, 90.00
R / Rfree (%) 16.9 / 19.7

Other elements in 2aqr:

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant (pdb code 2aqr). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant, PDB code: 2aqr:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 2aqr

Go back to Copper Binding Sites List in 2aqr
Copper binding site 1 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:14.3
occ:1.00
 NE2 A:HIS81 2.0 12.9 1.0
NE2 A:HIS160 2.0 10.5 1.0
ND1 A:HIS79 2.1 13.1 1.0
CD2 A:HIS160 2.9 11.4 1.0
CE1 A:HIS81 3.0 12.5 1.0
CE1 A:HIS79 3.0 11.0 1.0
CD2 A:HIS81 3.0 13.4 1.0
CE1 A:HIS160 3.1 11.1 1.0
CG A:HIS79 3.1 11.8 1.0
NE2 A:HIS104 3.3 12.2 1.0
CB A:HIS79 3.5 11.7 1.0
CD2 A:HIS104 3.6 11.1 1.0
CB A:MET158 3.8 11.9 1.0
O A:HOH382 3.8 17.6 1.0
CG A:MET158 4.0 14.8 1.0
ND1 A:HIS81 4.1 11.8 1.0
CG A:HIS160 4.1 11.8 1.0
CG A:HIS81 4.2 12.6 1.0
CE1 A:HIS104 4.2 11.5 1.0
NE2 A:HIS79 4.2 11.0 1.0
ND1 A:HIS160 4.2 11.8 1.0
O A:HOH352 4.2 17.5 1.0
CD2 A:HIS79 4.2 11.0 1.0
N A:HIS79 4.3 9.7 1.0
CA A:HIS79 4.4 9.5 1.0
O A:HIS79 4.6 9.8 1.0
CG A:HIS104 4.6 11.9 1.0
C A:HIS79 4.7 9.2 1.0
O A:MET158 4.7 11.3 1.0
ND1 A:HIS104 4.9 10.4 1.0
CA A:MET158 4.9 12.2 1.0
C A:MET158 5.0 10.4 1.0

Copper binding site 2 out of 5 in 2aqr

Go back to Copper Binding Sites List in 2aqr
Copper binding site 2 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu250

b:22.7
occ:1.00
 OE1 A:GLU73 1.9 26.6 1.0
OE1 B:GLU73 2.0 24.5 1.0
ND1 A:HIS133 2.1 21.9 1.0
ND1 B:HIS133 2.1 20.7 1.0
CD A:GLU73 2.6 22.0 1.0
OE2 A:GLU73 2.7 25.7 1.0
CD B:GLU73 2.8 26.0 1.0
OE2 B:GLU73 3.0 29.2 1.0
CE1 A:HIS133 3.0 22.2 1.0
CE1 B:HIS133 3.0 21.7 1.0
CG A:HIS133 3.0 20.4 1.0
CG B:HIS133 3.1 19.7 1.0
CB A:HIS133 3.4 19.2 1.0
CB B:HIS133 3.5 17.3 1.0
CG A:GLU73 4.0 24.2 1.0
CA A:HIS133 4.0 18.7 1.0
CA B:HIS133 4.1 17.0 1.0
NE2 A:HIS133 4.1 22.6 1.0
NE2 B:HIS133 4.1 22.5 1.0
CD2 A:HIS133 4.1 22.3 1.0
CD2 B:HIS133 4.2 20.4 1.0
CG B:GLU73 4.3 23.7 1.0
O A:HOH394 4.4 19.1 1.0
CB B:GLU73 4.8 20.4 1.0
N A:HIS133 4.8 16.1 1.0
N B:HIS133 4.9 15.3 1.0
O C:HOH387 4.9 29.9 1.0
O B:HOH419 4.9 26.7 1.0
CB A:GLU73 5.0 19.3 1.0

Copper binding site 3 out of 5 in 2aqr

Go back to Copper Binding Sites List in 2aqr
Copper binding site 3 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:14.5
occ:1.00
 NE2 B:HIS81 2.0 11.7 1.0
NE2 B:HIS160 2.1 11.2 1.0
ND1 B:HIS79 2.1 12.4 1.0
CE1 B:HIS81 3.0 12.6 1.0
CD2 B:HIS160 3.0 10.8 1.0
CE1 B:HIS79 3.0 11.1 1.0
CD2 B:HIS81 3.1 9.8 1.0
CG B:HIS79 3.1 11.2 1.0
CE1 B:HIS160 3.1 11.5 1.0
NE2 B:HIS104 3.2 14.5 1.0
CB B:HIS79 3.4 12.4 1.0
CD2 B:HIS104 3.5 13.8 1.0
O B:HOH474 3.7 26.0 1.0
CB B:MET158 3.8 12.7 1.0
CG B:MET158 4.0 13.5 1.0
CE1 B:HIS104 4.1 14.8 1.0
ND1 B:HIS81 4.1 10.7 1.0
NE2 B:HIS79 4.1 9.7 1.0
CG B:HIS160 4.1 11.1 1.0
ND1 B:HIS160 4.2 11.3 1.0
CG B:HIS81 4.2 9.6 1.0
CD2 B:HIS79 4.2 10.9 1.0
O B:HOH384 4.2 19.9 1.0
N B:HIS79 4.2 10.8 1.0
CA B:HIS79 4.3 11.2 1.0
CG B:HIS104 4.6 14.9 1.0
O B:HIS79 4.6 11.9 1.0
C B:HIS79 4.7 12.0 1.0
O B:MET158 4.7 12.1 1.0
ND1 B:HIS104 4.8 11.8 1.0
C B:MET158 5.0 12.3 1.0
CA B:MET158 5.0 12.8 1.0

Copper binding site 4 out of 5 in 2aqr

Go back to Copper Binding Sites List in 2aqr
Copper binding site 4 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu200

b:14.2
occ:1.00
 NE2 C:HIS81 2.0 10.8 1.0
ND1 C:HIS79 2.1 10.7 1.0
NE2 C:HIS160 2.1 12.0 1.0
CD2 C:HIS160 3.0 14.0 1.0
CE1 C:HIS79 3.0 8.6 1.0
CE1 C:HIS81 3.0 12.2 1.0
CD2 C:HIS81 3.1 10.6 1.0
CG C:HIS79 3.1 9.4 1.0
CE1 C:HIS160 3.2 15.2 1.0
NE2 C:HIS104 3.3 12.5 1.0
CB C:HIS79 3.5 10.6 1.0
CD2 C:HIS104 3.6 13.2 1.0
O C:HOH403 3.7 23.7 1.0
CB C:MET158 3.8 12.3 1.0
CG C:MET158 4.0 13.7 1.0
ND1 C:HIS81 4.1 10.7 1.0
NE2 C:HIS79 4.1 10.3 1.0
CE1 C:HIS104 4.2 12.1 1.0
CG C:HIS160 4.2 13.3 1.0
CG C:HIS81 4.2 8.8 1.0
CD2 C:HIS79 4.2 8.4 1.0
ND1 C:HIS160 4.2 13.5 1.0
O C:HOH420 4.3 23.8 1.0
N C:HIS79 4.3 10.3 1.0
CA C:HIS79 4.4 10.0 1.0
O C:HIS79 4.6 9.8 1.0
CG C:HIS104 4.6 13.2 1.0
O C:MET158 4.7 12.5 1.0
C C:HIS79 4.7 10.2 1.0
ND1 C:HIS104 4.9 11.8 1.0
C C:MET158 5.0 12.1 1.0
CA C:MET158 5.0 12.7 1.0

Copper binding site 5 out of 5 in 2aqr

Go back to Copper Binding Sites List in 2aqr
Copper binding site 5 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu251

b:19.7
occ:0.50
 OE1 C:GLU73 1.8 31.9 1.0
ND1 C:HIS133 2.0 19.7 1.0
CD C:GLU73 2.6 27.0 1.0
OE2 C:GLU73 2.8 32.1 1.0
CE1 C:HIS133 2.9 19.8 1.0
CG C:HIS133 3.1 18.0 1.0
CB C:HIS133 3.5 17.4 1.0
CG C:GLU73 4.0 28.0 1.0
NE2 C:HIS133 4.1 19.2 1.0
CA C:HIS133 4.1 18.2 1.0
CD2 C:HIS133 4.2 18.9 1.0
O C:HOH378 4.5 24.0 1.0
N C:HIS133 4.9 16.2 1.0
CB C:GLU73 5.0 22.9 1.0
O B:HOH431 5.0 27.2 1.0
O B:HOH417 5.0 24.1 1.0

Reference:

M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff. Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant To Be Published.
Page generated: Tue Jul 30 23:11:51 2024

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