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Crystal structure of the CU,MO-co dehydrogenase (codh); dithionite reduced state

Analyse Crystal structure of the CU,MO-co dehydrogenase (codh); dithionite reduced state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1N61
Type
protein
Length
2,491 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P19921, P19919, P19920

Structure

x-ray diffraction · 6 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein161—P19921
B—protein804—P19919
C—protein287—P19920
D—protein158—P19921
E—protein795—P19919
F—protein286—P19920

Compared structures

  • 1N61 · Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state · the same entry in another collection · chain F against F, TM-score 1.00
  • P19920 · AlphaFold monomer V2.0 prediction for carbon monoxide dehydrogenase medium chain (P19920) · a predicted model of the same protein · chain C against A, TM-score 1.00
  • P19919 · AlphaFold monomer V2.0 prediction for carbon monoxide dehydrogenase large chain (P19919) · a predicted model of the same protein · chain B against A, TM-score 1.00
  • P19921 · AlphaFold monomer V2.0 prediction for carbon monoxide dehydrogenase small chain (P19921) · a predicted model of the same protein · chain D against A, TM-score 0.99

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