Atomistry » Copper » PDB 1tmx-1x9l » 2bw4
Atomistry »
  Copper »
    PDB 1tmx-1x9l »
      2bw4 »

Copper in PDB 2bw4: Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase

Enzymatic activity of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase

All present enzymatic activity of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase:
1.7.2.1;

Protein crystallography data

The structure of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase, PDB code: 2bw4 was solved by S.V.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) 19.48 / 0.90
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 95.414, 95.414, 95.414, 90.00, 90.00, 90.00
R / Rfree (%) 11.7 / 13.4

Copper Binding Sites:

The binding sites of Copper atom in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase (pdb code 2bw4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase, PDB code: 2bw4:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2bw4

Go back to Copper Binding Sites List in 2bw4
Copper binding site 1 out of 2 in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:5.5
occ:1.00
ND1 A:HIS145 2.0 5.3 1.0
ND1 A:HIS95 2.0 5.2 1.0
SG A:CYS136 2.2 5.5 1.0
SD A:MET150 2.5 5.5 1.0
CE1 A:HIS145 3.0 6.0 1.0
CE1 A:HIS95 3.0 5.4 1.0
CG A:HIS95 3.1 5.4 1.0
CG A:HIS145 3.1 5.1 1.0
CB A:CYS136 3.2 5.0 1.0
CE A:MET150 3.3 6.7 1.0
CB A:HIS95 3.5 5.0 1.0
CB A:HIS145 3.5 4.7 1.0
CA A:HIS95 3.8 5.0 1.0
CG A:MET150 3.9 5.3 1.0
NE2 A:HIS145 4.1 6.6 1.0
NE2 A:HIS95 4.2 5.3 1.0
CD2 A:HIS145 4.2 6.5 1.0
CD2 A:HIS95 4.2 5.5 1.0
O A:LEU94 4.3 7.3 1.0
CG A:PRO138 4.3 6.7 1.0
CB A:MET150 4.4 4.9 1.0
SD A:MET62 4.4 6.7 0.9
CA A:CYS136 4.6 4.4 1.0
CD A:PRO138 4.6 5.5 1.0
N A:ASN96 4.7 5.0 1.0
CA A:HIS145 4.7 4.4 1.0
N A:HIS95 4.9 5.7 1.0
C A:HIS95 4.9 5.7 1.0
CB A:MET62 4.9 5.8 0.9
C A:LEU94 5.0 6.7 1.0
CB A:MET62 5.0 5.5 0.1

Copper binding site 2 out of 2 in 2bw4

Go back to Copper Binding Sites List in 2bw4
Copper binding site 2 out of 2 in the Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Atomic Resolution Structure of Resting State of the Achromobacter Cycloclastes Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:5.3
occ:0.90
NE2 A:HIS135 2.0 5.8 1.0
NE2 A:HIS100 2.0 5.2 1.0
O A:HOH2276 2.2 5.8 0.9
CE1 A:HIS100 2.9 4.7 1.0
CD2 A:HIS135 2.9 5.7 1.0
CE1 A:HIS135 3.0 5.5 1.0
CD2 A:HIS100 3.1 4.5 1.0
OD2 A:ASP98 3.8 11.5 0.5
ND1 A:HIS100 4.1 3.9 1.0
CG A:HIS135 4.1 4.4 1.0
ND1 A:HIS135 4.2 4.8 1.0
O A:HOH2277 4.2 21.6 1.0
O A:HOH2275 4.2 7.9 0.3
CG A:HIS100 4.2 3.8 1.0
CG A:ASP98 4.4 6.9 0.5
OD1 A:ASP98 4.7 7.0 0.5
OD2 A:ASP98 5.0 6.0 0.3

Reference:

S.V.Antonyuk, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain. Atomic Resolution Structures of Resting-State, Substrate- and Product-Complexed Cu-Nitrite Reductase Provide Insight Into Catalytic Mechanism Proc.Natl.Acad.Sci.Usa V. 102 12041 2005.
ISSN: ISSN 0027-8424
PubMed: 16093314
DOI: 10.1073/PNAS.0504207102
Page generated: Thu Sep 3 16:31:30 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy