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Human HSP90_MC domain structure

Analyse Human HSP90_MC domain structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RY1
Type: protein
Length: 1,207 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
EC: 3.6.4.10
UniProt: P07900
Ligands: MDC
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha (EC 3.6.4.10)	protein	405	43% helix, 17% strand	P07900
B	Heat shock protein HSP 90-alpha (EC 3.6.4.10)	protein	396	43% helix, 16% strand	P07900
C	Heat shock protein HSP 90-alpha (EC 3.6.4.10)	protein	406	44% helix, 17% strand	P07900

Ligands and binding sites

MDC · N-[2-(1-maleimidyl)ethyl]-7-diethylaminocoumarin-3-carboxamide · ligand · 3 copies · chains A, C, B

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	776	0.82	0.85	76	empty
2	464	0.74	0.83	54	MDC
3	532	0.73	0.81	47	MDC
4	409	0.67	0.80	54	empty
5	194	0.62	0.83	25	empty

Interfaces

3 interfaces between chains.

A–B · 1819 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 1800 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 480 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

7RY1 · human Hsp90_MC domain structure · the same entry in another collection · chain A against A, TM-score 1.00
P07900 · AlphaFold monomer V2.0 prediction for heat shock protein HSP 90-alpha (P07900) · 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 P07900
Elsewhere: RCSB PDB 7RY1 · PDBe 7RY1 · UniProt P07900

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