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Copper in PDB 1gs8: Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase

Enzymatic activity of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase

All present enzymatic activity of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8 was solved by M.J.Ellis, M.Prudencio, F.E.Dodd, 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) 68.97 / 1.9
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 79.636, 79.636, 99.867, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 20.7

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase (pdb code 1gs8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1gs8

Go back to Copper Binding Sites List in 1gs8
Copper binding site 1 out of 2 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1337

b:16.6
occ:1.00
ND1 A:HIS139 2.1 14.3 1.0
ND1 A:HIS89 2.2 10.6 1.0
SG A:CYS130 2.2 15.6 1.0
SD A:MET144 2.6 16.9 1.0
CE1 A:HIS89 3.1 12.8 1.0
CE1 A:HIS139 3.1 14.8 1.0
CG A:HIS89 3.2 11.5 1.0
CG A:HIS139 3.2 14.6 1.0
CB A:CYS130 3.3 13.6 1.0
CE A:MET144 3.5 12.8 1.0
CB A:HIS89 3.5 12.0 1.0
CB A:HIS139 3.5 12.6 1.0
CA A:HIS89 3.8 12.4 1.0
CG A:MET144 4.1 13.8 1.0
CG A:PRO132 4.1 14.8 1.0
O A:PRO88 4.1 15.1 1.0
NE2 A:HIS139 4.2 14.4 1.0
NE2 A:HIS89 4.2 14.2 1.0
CD2 A:HIS139 4.3 15.1 1.0
CD2 A:HIS89 4.3 11.8 1.0
CD A:PRO132 4.4 14.7 1.0
SD A:MET56 4.4 16.3 1.0
CB A:MET144 4.6 12.1 1.0
CA A:CYS130 4.7 11.8 1.0
CA A:HIS139 4.7 11.4 1.0
N A:ASN90 4.8 13.5 1.0
N A:HIS89 4.8 13.2 1.0
C A:HIS89 4.8 14.3 1.0
C A:PRO88 4.9 15.7 1.0

Copper binding site 2 out of 2 in 1gs8

Go back to Copper Binding Sites List in 1gs8
Copper binding site 2 out of 2 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1338

b:14.6
occ:1.00
NE2 A:HIS129 2.1 11.8 1.0
NE2 A:HIS94 2.1 10.9 1.0
O A:HOH2090 2.3 16.9 1.0
CD2 A:HIS129 3.0 10.7 1.0
CE1 A:HIS94 3.0 10.4 1.0
CE1 A:HIS129 3.2 12.8 1.0
CD2 A:HIS94 3.2 10.5 1.0
ND2 A:ASN92 3.6 14.1 1.0
O A:HOH2091 4.1 40.3 1.0
CG A:HIS129 4.1 11.2 1.0
ND1 A:HIS94 4.2 9.7 1.0
ND1 A:HIS129 4.2 12.4 1.0
CG A:HIS94 4.3 10.6 1.0
CG A:ASN92 4.5 12.0 1.0
OD1 A:ASN92 4.8 12.2 1.0

Reference:

M.J.Ellis, M.Prudencio, F.E.Dodd, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain. Biochemical and Crystallographic Studies of the MET144ALA, ASP92ASN and HIS254PHE Mutants of the Nitrite Reductase From Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism. J.Mol.Biol. V. 316 51 2002.
ISSN: ISSN 0022-2836
PubMed: 11829502
DOI: 10.1006/JMBI.2001.5304
Page generated: Thu Sep 3 15:57:02 2020
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