Research workbench
Full length TAH1 bound to yeast PIH1 and HSP90 peptide srmeevd
Analyse Full length TAH1 bound to yeast PIH1 and 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
- 4CGU
- Type
- protein
- Length
- 200 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25638, P38768, P07900
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 112 | — | P25638 |
| B | — | protein | 81 | — | P38768 |
| C | — | protein | 7 | — | P07900 |
Compared structures
- 4CGU · Full length Tah1 bound to yeast PIH1 and HSP90 peptide SRMEEVD · the same entry in another collection · chain A against A, TM-score 1.00
- P38768 · AlphaFold monomer V2.0 prediction for protein interacting with HSP90 1 (P38768) · a predicted model of the same protein · chain B against A, TM-score 0.87
- 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 0.82
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 P38768
- Every structure of UniProt P07900
- Elsewhere: RCSB PDB 4CGU · PDBe 4CGU · UniProt P25638 · UniProt P38768 · UniProt P07900
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