Research workbench
Full length TAH1 bound to HSP90 peptide srmeevd
Analyse Full length TAH1 bound to HSP90 peptide srmeevd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CGQ
- Type
- protein
- Length
- 98 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tpr repeat-containing protein associated with HSP90; Heat shock protein HSP 90-alpha
- UniProt
- P25638, P07900
- Ligands
- CL
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tpr repeat-containing protein associated with HSP90 | protein | 91 | 75% helix, 0% strand | P25638 |
| Q | Heat shock protein HSP 90-alpha | protein | 7 | 0% helix, 0% strand | P07900 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.36 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–Q · 325 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4CGQ · Full length Tah1 bound to HSP90 peptide SRMEEVD · the same entry in another collection · chain A against A, TM-score 1.00
- P25638 · AlphaFold monomer V2.0 prediction for tpr repeat-containing protein associated with HSP90… · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P25638
- Every structure of UniProt P07900
- Elsewhere: RCSB PDB 4CGQ · PDBe 4CGQ · UniProt P25638 · UniProt P07900
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