Research workbench
Structure of the 'minimal scaffold' (ms) domain of STE5 that cocatalyzes FUS3 phosphorylation by STE7
Analyse Structure of the 'minimal scaffold' (ms) domain of STE5 that cocatalyzes FUS3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FZE
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein STE5
- UniProt
- P32917
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein STE5 | protein | 185 | 38% helix, 21% strand | P32917 |
Compared structures
- 3FZE · Structure of the 'minimal scaffold' (ms) domain of Ste5 that cocatalyzes Fus3… · 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 0.88
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 3FZE · PDBe 3FZE · UniProt P32917
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