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Copper in PDB 4o65: Crystal Structure of the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii

Protein crystallography data

The structure of Crystal Structure of the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii, PDB code: 4o65 was solved by T.J.Lawton, J.Ham, T.Sun, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.43 / 1.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.886, 47.886, 192.614, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 22.9

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii (pdb code 4o65). 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 the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii, PDB code: 4o65:

Copper binding site 1 out of 1 in 4o65

Go back to Copper Binding Sites List in 4o65
Copper binding site 1 out of 1 in the Crystal Structure of the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii


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 the Cupredoxin Domain of Amob From Nitrosocaldus Yellowstonii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:36.5
occ:0.70
ND1 A:HIS156 1.9 35.4 1.0
NE2 A:HIS158 2.0 22.5 1.0
O A:HOH465 2.1 44.3 1.0
CG A:HIS156 2.9 34.0 1.0
CE1 A:HIS156 2.9 38.0 1.0
CD2 A:HIS158 3.0 21.6 1.0
CE1 A:HIS158 3.0 22.4 1.0
CB A:HIS156 3.3 29.7 1.0
O A:HIS156 3.8 24.2 1.0
NE2 A:HIS156 4.0 38.4 1.0
C A:HIS156 4.1 22.7 1.0
CD2 A:HIS156 4.1 36.7 1.0
ND1 A:HIS158 4.1 21.2 1.0
CG A:HIS158 4.2 19.7 1.0
CA A:HIS156 4.3 23.9 1.0
CA A:GLY173 4.5 27.8 1.0
N A:ALA157 4.9 20.3 1.0

Reference:

T.J.Lawton, J.Ham, T.Sun, A.C.Rosenzweig. Structural Conservation of the B Subunit in the Ammonia Monooxygenase/Particulate Methane Monooxygenase Superfamily. Proteins V. 82 2263 2014.
ISSN: ISSN 0887-3585
PubMed: 24523098
DOI: 10.1002/PROT.24535
Page generated: Sun Dec 13 11:15:25 2020

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