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Crystal structure of full-length htpg, the escherichia COLI HSP90

Analyse Crystal structure of full-length htpg, the escherichia COLI HSP90 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IOQ
Type: protein
Length: 1,144 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein htpg
UniProt: P0A6Z3
Pockets: 9 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein htpg	protein	567	39% helix, 20% strand	P0A6Z3
B	Chaperone protein htpg	protein	577	41% helix, 19% strand	P0A6Z3

Pockets

9 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	817	0.83	0.85	92	empty
2	803	0.80	0.83	87	empty
3	404	0.61	0.76	44	empty
4	86	0.54	0.85	30	empty
5	71	0.47	0.83	21	empty

Interfaces

1 interface between chains.

A–B · 437 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2IOQ · Crystal Structure of full-length HTPG, the Escherichia coli HSP90 · the same entry in another collection · chain A against A, TM-score 1.00
P0A6Z3 · AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P0A6Z3
Elsewhere: RCSB PDB 2IOQ · PDBe 2IOQ · UniProt P0A6Z3

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