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Anaerobic cobalt chelatase in cobalamin biosynthesis from salmonella typhimurium

Analyse Anaerobic cobalt chelatase in cobalamin biosynthesis from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QGO
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anaerobic cobalamin biosynthetic cobalt chelatase
UniProt: Q05592
Ligands: SO4
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anaerobic cobalamin biosynthetic cobalt chelatase	protein	257	49% helix, 18% strand	Q05592

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	321	0.68	0.82	33	SO4

Compared structures

1QGO · Anaerobic cobalt chelatase in cobalamin biosynthesis from salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
Q05592 · AlphaFold monomer V2.0 prediction for sirohydrochlorin cobaltochelatase (Q05592) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q05592
Elsewhere: RCSB PDB 1QGO · PDBe 1QGO · UniProt Q05592

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