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Copper in PDB 2aza: Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules

Protein crystallography data

The structure of Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules, PDB code: 2aza was solved by E.N.Baker, G.E.Norris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 75.000, 74.200, 99.500, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules (pdb code 2aza). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules, PDB code: 2aza:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2aza

Go back to Copper Binding Sites List in 2aza
Copper binding site 1 out of 2 in the Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu130

b:12.3
occ:1.00
ND1 A:HIS117 2.0 9.7 1.0
ND1 A:HIS46 2.1 11.6 1.0
SG A:CYS112 2.1 10.8 1.0
CG A:HIS117 3.0 10.6 1.0
CE1 A:HIS117 3.0 5.8 1.0
CG A:HIS46 3.0 7.7 1.0
CE1 A:HIS46 3.1 4.6 1.0
SD A:MET121 3.1 13.1 1.0
O A:GLY45 3.2 12.1 1.0
CB A:CYS112 3.2 8.6 1.0
CB A:HIS117 3.3 11.6 1.0
CB A:HIS46 3.5 10.4 1.0
CA A:HIS46 3.5 11.9 1.0
CE A:MET121 3.7 8.9 1.0
CB A:PHE114 3.9 7.5 1.0
C A:GLY45 4.0 10.0 1.0
CD2 A:HIS117 4.1 9.7 1.0
NE2 A:HIS117 4.1 9.6 1.0
N A:HIS46 4.2 9.2 1.0
NE2 A:HIS46 4.2 13.7 1.0
CD2 A:HIS46 4.2 9.6 1.0
CA A:CYS112 4.5 10.7 1.0
N A:ASN47 4.5 13.0 1.0
CG A:MET121 4.6 16.4 1.0
C A:HIS46 4.7 9.9 1.0
CG A:PHE114 4.7 10.4 1.0
N A:PHE114 4.8 14.9 1.0
C A:CYS112 4.9 13.6 1.0
CA A:HIS117 4.9 7.0 1.0
CB A:MET121 4.9 14.7 1.0
CA A:PHE114 5.0 11.1 1.0

Copper binding site 2 out of 2 in 2aza

Go back to Copper Binding Sites List in 2aza
Copper binding site 2 out of 2 in the Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Azurin From Alcaligenes Denitrificans. Refinement at 1.8 Angstroms Resolution and Comparison of the Two Crystallographically Independent Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu130

b:12.7
occ:1.00
ND1 B:HIS117 2.0 10.8 1.0
ND1 B:HIS46 2.1 12.9 1.0
SG B:CYS112 2.2 12.8 1.0
CE1 B:HIS117 3.0 8.1 1.0
CG B:HIS117 3.0 11.2 1.0
CE1 B:HIS46 3.0 7.6 1.0
O B:GLY45 3.1 11.2 1.0
SD B:MET121 3.1 14.5 1.0
CG B:HIS46 3.1 7.6 1.0
CB B:CYS112 3.2 5.7 1.0
CB B:HIS117 3.4 9.2 1.0
CA B:HIS46 3.4 6.4 1.0
CB B:HIS46 3.6 8.6 1.0
CB B:PHE114 3.9 8.6 1.0
C B:GLY45 4.0 13.3 1.0
CE B:MET121 4.0 9.5 1.0
NE2 B:HIS117 4.1 11.7 1.0
CD2 B:HIS117 4.1 12.6 1.0
N B:HIS46 4.1 13.9 1.0
NE2 B:HIS46 4.2 8.4 1.0
CD2 B:HIS46 4.2 9.0 1.0
N B:ASN47 4.5 10.1 1.0
C B:HIS46 4.5 11.0 1.0
CA B:CYS112 4.6 10.7 1.0
CG B:MET121 4.7 16.3 1.0
CG B:PHE114 4.7 10.5 1.0
CA B:HIS117 4.9 9.1 1.0
C B:CYS112 5.0 12.3 1.0

Reference:

E.N.Baker, E.N.Baker, G.E.Norris. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 3210236
DOI: 10.1016/0022-2836(88)90129-5
Page generated: Mon Jul 14 00:45:59 2025

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