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Copper in PDB 2vov: An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA

Protein crystallography data

The structure of An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA, PDB code: 2vov was solved by R.Helland, A.Fjellbirkeland, O.A.Karlsen, T.Ve, J.R.Lillehaug, H.B.Jensen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.30 / 1.35
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 72.990, 88.570, 101.430, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 21.1

Other elements in 2vov:

The structure of An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA (pdb code 2vov). 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 An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA, PDB code: 2vov:

Copper binding site 1 out of 1 in 2vov

Go back to Copper Binding Sites List in 2vov
Copper binding site 1 out of 1 in the An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of An Oxidized Tryptophan Facilitates Copper-Binding in Methylococcus Capsulatus Secreted Protein Mope. the Structure of Wild-Type Mope to 1.35AA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1339

b:10.2
occ:0.60
ND1 A:HIS132 2.0 15.5 1.0
ND1 A:HIS203 2.1 11.5 1.0
O A:HOH2137 2.5 27.5 1.0
CE1 A:HIS132 3.0 14.3 1.0
CG A:HIS132 3.0 8.6 1.0
N1 A:KYN130 3.1 15.0 1.0
CG A:HIS203 3.1 14.4 1.0
CE1 A:HIS203 3.1 37.9 1.0
CB A:HIS203 3.3 11.0 1.0
CB A:HIS132 3.4 12.0 1.0
CA A:HIS203 3.7 10.4 1.0
O A:HIS203 3.8 9.7 1.0
NE2 A:HIS132 4.1 14.8 1.0
N A:HIS132 4.1 10.0 1.0
CD2 A:HIS132 4.1 12.6 1.0
NE2 A:HIS203 4.2 7.8 1.0
CD2 A:HIS203 4.2 14.2 1.0
C A:HIS203 4.2 10.4 1.0
CG A:KYN130 4.4 12.4 1.0
CA A:HIS132 4.4 10.8 1.0
O2 A:KYN130 4.5 9.9 1.0
CB A:THR131 4.5 9.7 1.0
O A:HOH2218 4.7 28.5 1.0
N A:HIS203 4.9 10.0 1.0
C A:THR131 4.9 9.7 1.0
CG2 A:THR131 5.0 10.1 1.0

Reference:

R.Helland, A.Fjellbirkeland, O.A.Karlsen, T.Ve, J.R.Lillehaug, H.B.Jensen. An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus Capsulatus-Secreted Protein Mope. J.Biol.Chem. V. 283 13897 2008.
ISSN: ISSN 0021-9258
PubMed: 18348978
DOI: 10.1074/JBC.M800340200
Page generated: Sun Dec 13 11:07:10 2020

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