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Copper in PDB 6cxh: Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z

Enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z

All present enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z:
1.14.13.25;

Protein crystallography data

The structure of Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z, PDB code: 6cxh was solved by S.Y.Ro, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.58 / 2.70
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 143.840, 143.840, 146.152, 90.00, 90.00, 120.00
R / Rfree (%) 21.3 / 26.8

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z (pdb code 6cxh). 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 Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z, PDB code: 6cxh:

Copper binding site 1 out of 1 in 6cxh

Go back to Copper Binding Sites List in 6cxh
Copper binding site 1 out of 1 in the Crystal Structure of Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z


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 Particulate Methane Monooxygenase From Methylomicrobium Alcaliphilum 20Z within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:45.1
occ:1.00
 N A:HIS33 1.9 53.8 1.0
NE2 A:HIS139 2.1 37.6 1.0
ND1 A:HIS137 2.1 43.1 1.0
CA A:HIS33 2.5 59.5 1.0
ND1 A:HIS33 2.5 71.7 1.0
CD2 A:HIS139 2.8 32.8 1.0
CE1 A:HIS137 2.9 44.0 1.0
CG A:HIS137 3.2 35.2 1.0
CG A:HIS33 3.3 68.5 1.0
CE1 A:HIS139 3.3 37.8 1.0
CB A:HIS33 3.4 61.4 1.0
CE1 A:HIS33 3.6 73.7 1.0
CB A:HIS137 3.7 25.9 1.0
C A:HIS33 3.8 55.6 1.0
NE2 A:HIS137 4.0 42.1 1.0
O A:HIS137 4.1 35.4 1.0
CG A:HIS139 4.1 26.2 1.0
CD2 A:HIS137 4.1 42.3 1.0
ND1 A:HIS139 4.3 28.1 1.0
O A:HIS33 4.3 55.7 1.0
CD2 A:HIS33 4.5 72.8 1.0
OE1 A:GLU35 4.5 55.7 1.0
NE2 A:HIS33 4.6 72.2 1.0
N A:GLY34 4.7 47.1 1.0
C A:HIS137 4.7 26.1 1.0
OE2 A:GLU35 4.8 59.3 1.0
CA A:HIS137 4.8 26.2 1.0

Reference:

S.Y.Ro, M.O.Ross, Y.W.Deng, S.Batelu, T.J.Lawton, J.D.Hurley, T.L.Stemmler, B.M.Hoffman, A.C.Rosenzweig. From Micelles to Bicelles: Effect of the Membrane on Particulate Methane Monooxygenase Activity. J. Biol. Chem. V. 293 10457 2018.
ISSN: ESSN 1083-351X
PubMed: 29739854
DOI: 10.1074/JBC.RA118.003348
Page generated: Mon Jul 14 05:55:06 2025

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