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Conformation rearrangement of heat shock protein 90 upon ADP binding

Analyse Conformation rearrangement of heat shock protein 90 upon ADP binding in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y4U
Type: protein
Length: 926 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein htpg
UniProt: P0A6Z3
Pockets: 13 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein htpg	protein	472	38% helix, 24% strand	P0A6Z3
B	Chaperone protein htpg	protein	454	37% helix, 24% strand	P0A6Z3

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	636	0.75	0.81	83	empty
2	661	0.75	0.81	82	empty
3	809	0.74	0.79	68	empty
4	502	0.73	0.82	61	empty
5	473	0.69	0.80	53	empty

Interfaces

1 interface between chains.

A–B · 2410 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

1Y4U · Conformation rearrangement of heat shock protein 90 upon ADP binding · 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 B against A, TM-score 0.96

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 1Y4U · PDBe 1Y4U · UniProt P0A6Z3

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