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Copper in PDB 2bp8: M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans

Protein crystallography data

The structure of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans, PDB code: 2bp8 was solved by M.A.Hough, M.J.Ellis, S.Antonyuk, R.W.Strange, 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) 28.00 / 1.90
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 90.600, 90.600, 291.458, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 18.9

Other elements in 2bp8:

The structure of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans also contains other interesting chemical elements:

Zinc (Zn) 10 atoms

Copper Binding Sites:

The binding sites of Copper atom in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans (pdb code 2bp8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans, PDB code: 2bp8:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2bp8

Go back to Copper Binding Sites List in 2bp8
Copper binding site 1 out of 4 in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1337

b:17.6
occ:1.00
ND1 A:HIS139 2.0 18.5 1.0
SG A:CYS130 2.1 19.9 1.0
ND1 A:HIS89 2.2 18.3 1.0
OE1 A:GLN144 2.2 22.0 1.0
CE1 A:HIS139 3.0 18.5 1.0
CE1 A:HIS89 3.1 19.6 1.0
CG A:HIS139 3.1 16.2 1.0
CG A:HIS89 3.2 19.8 1.0
CB A:CYS130 3.2 18.9 1.0
CD A:GLN144 3.2 23.9 1.0
CB A:HIS139 3.5 15.1 1.0
CB A:HIS89 3.6 18.9 1.0
NE2 A:GLN144 3.6 28.2 1.0
CA A:HIS89 3.9 19.7 1.0
O A:PRO88 4.1 21.4 1.0
NE2 A:HIS139 4.1 17.1 1.0
CD2 A:HIS139 4.2 17.2 1.0
CG A:PRO132 4.2 22.4 1.0
NE2 A:HIS89 4.2 20.4 1.0
CD2 A:HIS89 4.3 18.9 1.0
CD A:PRO132 4.4 20.5 1.0
SD A:MET56 4.5 22.3 1.0
CG A:GLN144 4.5 21.1 1.0
CA A:CYS130 4.6 17.7 1.0
CA A:HIS139 4.8 14.7 1.0
N A:ASN90 4.8 17.9 1.0
N A:HIS89 4.9 20.6 1.0
C A:PRO88 4.9 21.9 1.0
CB A:GLN144 4.9 16.6 1.0
C A:HIS89 5.0 18.9 1.0

Copper binding site 2 out of 4 in 2bp8

Go back to Copper Binding Sites List in 2bp8
Copper binding site 2 out of 4 in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1338

b:13.5
occ:1.00
NE2 A:HIS129 2.0 12.6 1.0
NE2 A:HIS94 2.1 14.0 1.0
O A:HOH2177 2.1 16.4 1.0
CD2 A:HIS129 3.0 13.4 1.0
CE1 A:HIS94 3.0 16.2 1.0
CE1 A:HIS129 3.1 12.4 1.0
CD2 A:HIS94 3.2 11.7 1.0
OD2 A:ASP92 3.7 25.6 1.0
CG A:HIS129 4.1 13.4 1.0
ND1 A:HIS94 4.2 14.4 1.0
ND1 A:HIS129 4.2 13.4 1.0
CG A:HIS94 4.3 12.9 1.0
CG A:ASP92 4.4 19.4 1.0
OD1 A:ASP92 4.8 20.4 1.0
O A:HOH2179 4.9 19.8 1.0

Copper binding site 3 out of 4 in 2bp8

Go back to Copper Binding Sites List in 2bp8
Copper binding site 3 out of 4 in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1337

b:21.8
occ:1.00
ND1 B:HIS139 2.0 20.3 1.0
SG B:CYS130 2.2 24.0 1.0
OE1 B:GLN144 2.2 25.0 1.0
ND1 B:HIS89 2.3 23.4 1.0
CE1 B:HIS139 2.9 23.6 1.0
CG B:HIS139 3.1 19.5 1.0
CD B:GLN144 3.1 24.8 1.0
CE1 B:HIS89 3.2 25.2 1.0
CB B:CYS130 3.3 21.5 1.0
CG B:HIS89 3.3 25.3 1.0
NE2 B:GLN144 3.5 27.9 1.0
CB B:HIS139 3.5 17.9 1.0
CB B:HIS89 3.5 24.4 1.0
CA B:HIS89 3.9 24.6 1.0
NE2 B:HIS139 4.1 22.5 1.0
O B:PRO88 4.1 25.9 1.0
CD2 B:HIS139 4.2 22.9 1.0
CG B:PRO132 4.3 25.7 1.0
NE2 B:HIS89 4.3 25.4 1.0
CD B:PRO132 4.4 24.5 1.0
CD2 B:HIS89 4.4 25.1 1.0
SD B:MET56 4.4 23.9 1.0
CG B:GLN144 4.5 21.7 1.0
CA B:CYS130 4.7 20.7 1.0
CA B:HIS139 4.8 17.4 1.0
N B:ASN90 4.8 23.0 1.0
CB B:GLN144 4.9 18.9 1.0
N B:HIS89 4.9 25.2 1.0
C B:PRO88 4.9 25.8 1.0
C B:HIS89 5.0 24.4 1.0

Copper binding site 4 out of 4 in 2bp8

Go back to Copper Binding Sites List in 2bp8
Copper binding site 4 out of 4 in the M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of M144Q Structure of Nitrite Reductase From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1338

b:16.0
occ:1.00
O B:HOH2136 2.0 12.2 1.0
NE2 B:HIS129 2.1 15.4 1.0
NE2 B:HIS94 2.2 16.4 1.0
CE1 B:HIS129 3.0 16.8 1.0
CD2 B:HIS129 3.1 17.3 1.0
CE1 B:HIS94 3.1 16.9 1.0
CD2 B:HIS94 3.2 17.7 1.0
OD2 B:ASP92 3.9 29.8 1.0
ND1 B:HIS129 4.2 17.4 1.0
CG B:HIS129 4.2 17.1 1.0
ND1 B:HIS94 4.3 16.3 1.0
CG B:HIS94 4.3 15.1 1.0
CG B:ASP92 4.5 23.6 1.0
OD1 B:ASP92 4.8 24.5 1.0
O B:HOH2138 4.9 23.6 1.0

Reference:

M.A.Hough, M.J.Ellis, S.Antonyuk, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain. High Resolution Structural Studies of Mutants Provide Insights Into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase J.Mol.Biol. V. 350 300 2005.
ISSN: ISSN 0022-2836
PubMed: 15927201
DOI: 10.1016/J.JMB.2005.04.006
Page generated: Sun Dec 13 11:03:43 2020

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