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Copper in PDB 1gs7: Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

Enzymatic activity of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

All present enzymatic activity of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs7 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) 69.01 / 1.85
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 78.903, 78.903, 98.423, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 19.4

Other elements in 1gs7:

The structure of Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase (pdb code 1gs7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs7:

Copper binding site 1 out of 1 in 1gs7

Go back to Copper Binding Sites List in 1gs7
Copper binding site 1 out of 1 in the Crystal Structure of H254F Mutant of 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 H254F Mutant of Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1337

b:24.3
occ:1.00
ND1 A:HIS139 2.1 15.1 1.0
ND1 A:HIS89 2.2 16.0 1.0
SG A:CYS130 2.2 20.9 1.0
SD A:MET144 2.5 20.3 1.0
CE1 A:HIS139 3.1 15.0 1.0
CG A:HIS139 3.1 15.9 1.0
CE1 A:HIS89 3.1 16.8 1.0
CG A:HIS89 3.1 16.6 1.0
CB A:CYS130 3.2 17.0 1.0
CB A:HIS139 3.4 15.2 1.0
CE A:MET144 3.4 15.5 1.0
CB A:HIS89 3.4 16.2 1.0
CA A:HIS89 3.8 16.6 1.0
CG A:PRO132 4.0 17.8 1.0
CG A:MET144 4.1 16.6 1.0
O A:PRO88 4.1 18.6 1.0
NE2 A:HIS139 4.2 14.7 1.0
CD2 A:HIS139 4.2 14.8 1.0
NE2 A:HIS89 4.2 17.3 1.0
CD2 A:HIS89 4.3 16.0 1.0
CD A:PRO132 4.3 16.5 1.0
SD A:MET56 4.4 18.6 1.0
CB A:MET144 4.6 14.6 1.0
CA A:HIS139 4.7 14.0 1.0
CA A:CYS130 4.7 16.0 1.0
N A:ASN90 4.8 17.5 1.0
N A:HIS89 4.8 17.7 1.0
C A:HIS89 4.9 16.4 1.0
C A:PRO88 4.9 18.9 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: Sun Dec 13 10:59:02 2020

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