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Crystal structure of M. tuberculosis chaperonin-10

Analyse Crystal structure of M. tuberculosis chaperonin-10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HX5
Type: protein
Length: 574 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 10 kda chaperonin
UniProt: P09621
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	10 kda chaperonin	protein	82	4% helix, 49% strand	P09621

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	434	0.73	0.84	54	empty
2	199	0.65	0.85	24	empty
3	230	0.65	0.83	33	empty
4	245	0.63	0.82	38	empty
5	208	0.63	0.83	26	empty

Interfaces

7 interfaces between chains.

D–E · 842 Å² buried · 8 hydrogen bonds · protein-protein
D–F · 840 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 819 Å² buried · 8 hydrogen bonds · protein-protein
F–G · 803 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 793 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1HX5 · Crystal structure of M. tuberculosis chaperonin-10 · 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 P09621
Elsewhere: RCSB PDB 1HX5 · PDBe 1HX5 · UniProt P09621

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