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Copper in PDB 1y3j: Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein

Enzymatic activity of Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein

All present enzymatic activity of Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein:
3.6.3.4;

Copper Binding Sites:

The binding sites of Copper atom in the Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein (pdb code 1y3j). 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 Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein, PDB code: 1y3j:

Copper binding site 1 out of 1 in 1y3j

Go back to Copper Binding Sites List in 1y3j
Copper binding site 1 out of 1 in the Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Solution Structure of the Copper(I) Form of the Fifth Domain of Menkes Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu78

b:3.2
occ:1.00
SG A:CYS14 2.2 2.4 1.0
SG A:CYS17 2.2 3.0 1.0
O A:ALA15 2.6 2.6 1.0
H A:CYS17 2.7 2.1 1.0
HB3 A:CYS14 2.9 2.3 1.0
CB A:CYS14 3.1 1.5 1.0
CB A:CYS17 3.4 2.1 1.0
HB2 A:CYS17 3.4 1.8 1.0
HB2 A:SER16 3.5 3.1 1.0
N A:CYS17 3.6 1.9 1.0
C A:ALA15 3.8 1.7 1.0
C A:CYS14 3.9 1.4 1.0
CA A:CYS17 3.9 2.0 1.0
HB2 A:CYS14 3.9 2.8 1.0
HA A:CYS17 4.1 2.3 1.0
CA A:CYS14 4.1 1.4 1.0
N A:ALA15 4.2 2.0 1.0
O A:CYS14 4.2 2.3 1.0
HB3 A:CYS17 4.3 2.6 1.0
H A:ALA15 4.3 2.8 1.0
CB A:SER16 4.6 2.6 1.0
HA A:CYS14 4.6 1.4 1.0
C A:SER16 4.7 1.8 1.0
CA A:ALA15 4.7 2.3 1.0
HE2 A:PHE66 4.7 4.5 1.0
N A:SER16 4.8 1.4 1.0
CA A:SER16 4.9 1.8 1.0

Reference:

L.Banci, I.Bertini, S.Ciofi-Baffoni, C.T.Chasapis, N.Hadjiliadis, A.Rosato. An uc(Nmr) Study of the Interaction Between the Human Copper(I) Chaperone and the Second and Fifth Metal-Binding Domains of the Menkes Protein Febs J. V. 272 865 2005.
ISSN: ISSN 1742-464X
PubMed: 15670166
DOI: 10.1111/J.1742-4658.2004.04526.X
Page generated: Wed Oct 28 14:18:13 2020
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