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Catalytic subunit of cobaltochelatase from mycobacterium tuberculosis

Analyse Catalytic subunit of cobaltochelatase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C6O
Type: protein
Length: 1,173 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cobalamin biosynthesis protein cobn
EC: 6.6.1.2
UniProt: A0A0T5XW27
Ligands: NA
Pockets: 14 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cobalamin biosynthesis protein cobn (EC 6.6.1.2)	protein	1173	50% helix, 14% strand	A0A0T5XW27

Ligands and binding sites

NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	929	0.82	0.84	87	empty
2	325	0.78	0.89	55	GOL
3	237	0.66	0.84	37	GOL
4	129	0.51	0.80	22	empty
5	161	0.49	0.77	29	empty

Compared structures

7C6O · Catalytic Subunit of Cobaltochelatase from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0T5XW27
Elsewhere: RCSB PDB 7C6O · PDBe 7C6O · UniProt A0A0T5XW27

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