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Crystal structure of desulfovibrio vulgaris carbon monoxide dehydrogenase with the D-cluster ligating cysteines mutated to alanines, coexpressed with cooc, as-isolated

Analyse Crystal structure of desulfovibrio vulgaris carbon monoxide dehydrogenase with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ONS
Type
protein
Length
621 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbon monoxide dehydrogenase
EC
1.2.7.4
UniProt
A0A0E0T3I2
Ligands
SF4, XCC
Pockets
5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbon monoxide dehydrogenase (EC 1.2.7.4)protein62152% helix, 11% strandA0A0E0T3I2

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · chains A
  • XCC · FE(4)-NI(1)-S(4) cluster · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1610.730.9825empty
2660.490.8517empty
31710.440.7429empty
4530.330.7712empty
5570.270.7313empty

Compared structures

  • 6ONS · Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase with the… · the same entry in another collection · chain A against A, TM-score 1.00

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