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Copper in PDB 2wtp: Crystal Structure of Cu-Form Czce From C. Metallidurans CH34

Protein crystallography data

The structure of Crystal Structure of Cu-Form Czce From C. Metallidurans CH34, PDB code: 2wtp was solved by I.Haertlein, E.Girard, G.Sarret, J.Hazemann, P.Gourhant, R.Kahn, J.Coves, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.141 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 105.000, 29.530, 71.170, 90.00, 113.41, 90.00
R / Rfree (%) 15.99 / 18.85

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Cu-Form Czce From C. Metallidurans CH34 (pdb code 2wtp). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Cu-Form Czce From C. Metallidurans CH34, PDB code: 2wtp:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 2wtp

Go back to Copper Binding Sites List in 2wtp
Copper binding site 1 out of 3 in the Crystal Structure of Cu-Form Czce From C. Metallidurans CH34


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 Cu-Form Czce From C. Metallidurans CH34 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1109

b:21.7
occ:0.20
ND1 A:HIS24 2.2 17.1 1.0
CE1 A:HIS24 3.0 14.1 1.0
O A:HOH2006 3.1 48.6 1.0
CG A:HIS24 3.3 12.1 1.0
CB A:HIS24 3.7 12.1 1.0
CA A:HIS24 4.1 12.5 1.0
CD1 A:LEU27 4.1 21.8 1.0
O A:HOH2016 4.2 29.3 1.0
NE2 A:HIS24 4.2 15.5 1.0
O A:HOH2004 4.2 41.7 1.0
CD2 A:HIS24 4.3 15.8 1.0

Copper binding site 2 out of 3 in 2wtp

Go back to Copper Binding Sites List in 2wtp
Copper binding site 2 out of 3 in the Crystal Structure of Cu-Form Czce From C. Metallidurans CH34


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 Cu-Form Czce From C. Metallidurans CH34 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1108

b:13.3
occ:0.65
N B:TRS1105 1.9 12.4 0.5
OD1 B:ASP100 1.9 18.3 1.0
O1 B:TRS1105 1.9 24.9 0.5
OD2 A:ASP100 2.1 19.1 1.0
N B:TRS1105 2.2 12.4 0.2
O3 B:TRS1105 2.7 18.9 0.5
O B:HOH2089 2.7 29.8 1.0
C B:TRS1105 2.8 14.7 0.5
CG B:ASP100 2.8 22.8 1.0
CG A:ASP100 2.9 18.3 1.0
O3 B:TRS1105 2.9 18.9 0.2
C1 B:TRS1105 2.9 19.8 0.5
C B:TRS1105 2.9 14.7 0.2
OD1 A:ASP100 3.0 16.2 1.0
C1 B:TRS1105 3.0 19.8 0.2
OD2 B:ASP100 3.0 22.4 1.0
C3 B:TRS1105 3.2 13.2 0.5
MG A:MG1110 3.3 15.2 0.7
C3 B:TRS1105 3.3 13.2 0.2
O A:HOH2055 3.4 17.2 1.0
O B:HOH2088 3.5 32.4 1.0
OD1 B:ASP77 3.9 19.1 1.0
C2 B:TRS1105 4.1 20.5 0.5
CB B:ASP100 4.2 14.0 1.0
C2 B:TRS1105 4.2 20.5 0.2
CB A:ASP100 4.3 11.7 1.0
O1 B:TRS1105 4.3 24.9 0.2
O A:HOH2096 4.3 18.9 0.8
O A:ARG101 4.3 9.9 1.0
OD2 B:ASP77 4.4 21.7 1.0
O2 B:TRS1105 4.4 37.3 0.2
CG B:ASP77 4.5 19.7 1.0
O A:HOH2060 4.6 13.5 1.0
N B:ARG101 4.6 13.8 1.0
CA B:ASP100 4.7 11.6 1.0
O B:HOH2087 4.8 26.1 0.8
O B:ARG101 4.9 17.4 1.0
O A:HOH2076 5.0 16.8 0.8

Copper binding site 3 out of 3 in 2wtp

Go back to Copper Binding Sites List in 2wtp
Copper binding site 3 out of 3 in the Crystal Structure of Cu-Form Czce From C. Metallidurans CH34


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Cu-Form Czce From C. Metallidurans CH34 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1109

b:37.7
occ:0.40
NE2 B:HIS24 1.8 32.8 1.0
CE1 B:HIS24 2.8 28.6 1.0
CD2 B:HIS24 2.9 40.5 1.0
ND1 B:HIS24 3.9 35.1 1.0
CG B:HIS24 4.0 30.1 1.0

Reference:

I.Petit-Haertlein, E.Girard, G.Sarret, J.Hazemann, P.Gourhant, R.Kahn, J.Coves. Evidence For Conformational Changes Upon Copper Binding to Cupriavidus Metallidurans Czce. Biochemistry V. 49 1913 2010.
ISSN: ISSN 0006-2960
PubMed: 20112954
DOI: 10.1021/BI100001Z
Page generated: Thu Sep 3 16:53:11 2020
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