Research workbench
Structure of the minimal STE5 vwa domain subject to autoinhibition by the STE5 pH domain
Analyse Structure of the minimal STE5 vwa domain subject to autoinhibition by the STE5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F2H
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32917
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 191 | — | P32917 |
Compared structures
- 4F2H · Structure of the minimal Ste5 VWA domain subject to autoinhibition by the Ste5 PH domain · the same entry in another collection · chain A against A, TM-score 1.00
- P32917 · AlphaFold monomer V2.0 prediction for protein STE5 (P32917) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P32917
- Elsewhere: RCSB PDB 4F2H · PDBe 4F2H · UniProt P32917
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