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Sirohydrochlorin nickelochelatase cfba in complex with CO2+ and formate

Analyse Sirohydrochlorin nickelochelatase cfba in complex with CO2+ and formate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M29
Type
protein
Length
244 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sirohydrochlorin cobaltochelatase
EC
4.99.1.3, 4.99.1.11
UniProt
Q58380
Ligands
CO
Pockets
2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSirohydrochlorin cobaltochelatase (EC 4.99.1.3, 4.99.1.11)protein12236% helix, 20% strandQ58380

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · 2 copies · chains A, B
  • FMT · Formic acid · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13820.770.8635CO, FMT
2500.270.7413empty

Interfaces

1 interface between chains.

  • A–B · 2079 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 6M29 · Sirohydrochlorin nickelochelatase CfbA in complex with Co2+ and formate · the same entry in another collection · chain A against A, TM-score 1.00
  • Q58380 · AlphaFold monomer V2.0 prediction for sirohydrochlorin cobaltochelatase (Q58380) · a predicted model of the same protein · chain A against A, TM-score 0.98

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