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Copper in PDB 2zoo: Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125

Enzymatic activity of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125

All present enzymatic activity of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125:
1.7.2.1; 1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125, PDB code: 2zoo was solved by M.Nojiri, A.Tsuda, K.Yamaguchi, S.Suzuki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.95
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 180.338, 180.338, 180.338, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 18.6

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 (pdb code 2zoo). 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 Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125, PDB code: 2zoo:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2zoo

Go back to Copper Binding Sites List in 2zoo
Copper binding site 1 out of 2 in the Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125


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 Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:17.9
occ:1.00
ND1 A:HIS133 2.1 17.1 1.0
ND1 A:HIS84 2.1 17.9 1.0
SG A:CYS125 2.2 18.4 1.0
SD A:MET138 2.5 17.7 1.0
CE1 A:HIS133 3.0 18.0 1.0
CG A:HIS133 3.1 18.6 1.0
CE1 A:HIS84 3.1 19.5 1.0
CG A:HIS84 3.1 18.1 1.0
CB A:CYS125 3.2 17.6 1.0
CE A:MET138 3.4 14.5 1.0
CB A:HIS84 3.5 18.2 1.0
CB A:HIS133 3.5 16.8 1.0
CA A:HIS84 3.8 19.1 1.0
O A:PRO83 4.0 18.3 1.0
NE2 A:HIS133 4.1 16.9 1.0
CG A:MET138 4.1 16.0 1.0
CD2 A:HIS133 4.1 16.5 1.0
NE2 A:HIS84 4.2 16.7 1.0
CD2 A:HIS84 4.3 17.4 1.0
CB A:THR127 4.3 17.2 1.0
OG1 A:THR127 4.3 17.2 1.0
CA A:HIS133 4.6 17.2 1.0
CE3 A:TRP51 4.6 14.8 1.0
CB A:MET138 4.6 15.8 1.0
CA A:CYS125 4.6 17.8 1.0
N A:ASN85 4.6 19.1 1.0
N A:HIS84 4.8 18.1 1.0
C A:HIS84 4.8 19.4 1.0
C A:PRO83 4.8 18.5 1.0

Copper binding site 2 out of 2 in 2zoo

Go back to Copper Binding Sites List in 2zoo
Copper binding site 2 out of 2 in the Crystal Structure of Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125


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 Nitrite Reductase From Pseudoalteromonas Haloplanktis TAC125 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:19.7
occ:1.00
NE2 A:HIS89 1.9 17.0 1.0
NE2 A:HIS124 2.0 17.7 1.0
O A:HOH1201 2.1 27.5 1.0
CE1 A:HIS89 2.9 17.0 1.0
CD2 A:HIS124 2.9 17.1 1.0
CD2 A:HIS89 3.0 16.4 1.0
CE1 A:HIS124 3.1 18.2 1.0
OD1 A:ASP87 3.9 22.9 1.0
ND1 A:HIS89 4.0 16.9 1.0
CG A:HIS124 4.1 18.4 1.0
CG A:HIS89 4.1 17.8 1.0
ND1 A:HIS124 4.1 16.9 1.0
CG A:ASP87 4.4 20.9 1.0
OD2 A:ASP87 4.7 20.4 1.0
CG2 A:ILE122 4.8 17.6 1.0
O A:HOH875 4.8 21.9 1.0

Reference:

M.Nojiri, H.Koteishi, A.Tsuda, T.Nakagami, K.Kobayashi, T.Inoue, K.Yamaguchi, S.Suzuki. Electron Transfer Processes Within and Between Proteins Containing the Heme C and Blue Cu To Be Published.
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