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Copper in PDB 6wti: The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli

Other elements in 6wti:

The structure of The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli (pdb code 6wti). 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 The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli, PDB code: 6wti:

Copper binding site 1 out of 1 in 6wti

Go back to Copper Binding Sites List in 6wti
Copper binding site 1 out of 1 in the The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Cryo-Em Structure of the Ubiquinol Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1003

b:32.5
occ:1.00
NE2 A:HIS334 1.9 24.3 1.0
ND1 A:HIS284 2.0 25.1 1.0
CE1 A:HIS334 2.3 24.3 1.0
CE1 A:HIS284 2.5 25.1 1.0
NE2 A:HIS333 2.6 24.3 1.0
CG A:HIS284 3.0 25.1 1.0
CD2 A:HIS334 3.2 24.3 1.0
CE1 A:HIS333 3.4 24.3 1.0
ND1 A:HIS334 3.5 24.3 1.0
NE2 A:HIS284 3.5 25.1 1.0
CD2 A:HIS333 3.6 24.3 1.0
CB A:HIS284 3.7 25.1 1.0
CD2 A:HIS284 3.8 25.1 1.0
CHA A:HEO1002 3.9 24.5 1.0
C1A A:HEO1002 3.9 24.5 1.0
CG A:HIS334 4.0 24.3 1.0
CA A:HIS284 4.1 25.1 1.0
NA A:HEO1002 4.1 24.5 1.0
C4D A:HEO1002 4.2 24.5 1.0
ND A:HEO1002 4.4 24.5 1.0
C2A A:HEO1002 4.5 24.5 1.0
ND1 A:HIS333 4.6 24.3 1.0
CG2 A:VAL287 4.7 24.8 1.0
CG A:HIS333 4.7 24.3 1.0
FE A:HEO1002 4.8 24.5 1.0
C4A A:HEO1002 4.8 24.5 1.0
C3D A:HEO1002 4.9 24.5 1.0

Reference:

C.C.Su, M.Lyu, C.E.Morgan, J.R.Bolla, C.V.Robinson, E.W.Yu. A 'Build and Retrieve' Methodology to Simultaneously Solve Cryo-Em Structures of Membrane Proteins. Nat.Methods V. 18 69 2021.
ISSN: ESSN 1548-7105
PubMed: 33408407
DOI: 10.1038/S41592-020-01021-2
Page generated: Wed Jul 31 07:46:02 2024

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