Research workbench

TPR2AB-DOMAIN:PHSP90-complex of yeast STI1

Analyse TPR2AB-DOMAIN:PHSP90-complex of yeast STI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UQ3
Type: protein
Length: 266 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein STI1; Heat shock protein
UniProt: P15705
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 3 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein STI1	protein	258	82% helix, 0% strand	P15705
B	Heat shock protein	protein	5	0% helix, 0% strand	—
C	Heat shock protein	protein	3	0% helix, 0% strand	—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.44	0.78	19	empty
2	75	0.34	0.75	14	empty

Interfaces

2 interfaces between chains.

A–B · 473 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 287 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3UQ3 · TPR2AB-domain:pHSP90-complex of yeast Sti1 · the same entry in another collection · chain A against A, TM-score 1.00
P15705 · AlphaFold monomer V2.0 prediction for heat shock protein STI1 (P15705) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P15705
Elsewhere: RCSB PDB 3UQ3 · PDBe 3UQ3 · UniProt P15705

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