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The structure of and photolytic induced changes of carbon monoxide binding to the cytochrome BA3-oxidase from thermus thermophilus

Analyse The structure of and photolytic induced changes of carbon monoxide binding to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QJT
Type: protein
Length: 756 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q5SJ79, Q5SJ80, P82543

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	557	—	Q5SJ79
B	—	protein	166	—	Q5SJ80
C	—	protein	33	—	P82543

Compared structures

3QJT · The structure of and photolytic induced changes of carbon monoxide binding to the… · the same entry in another collection · chain A against A, TM-score 1.00
Q5SJ79 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase subunit 1 (Q5SJ79) · a predicted model of the same protein · chain A against A, TM-score 0.99
Q5SJ80 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase subunit 2 (Q5SJ80) · a predicted model of the same protein · chain B against A, TM-score 0.99
P82543 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase polypeptide 2A (P82543) · a predicted model of the same protein · chain C against A, TM-score 0.83

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5SJ79
Every structure of UniProt Q5SJ80
Every structure of UniProt P82543
Elsewhere: RCSB PDB 3QJT · PDBe 3QJT · UniProt Q5SJ79 · UniProt Q5SJ80 · UniProt P82543

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