Research workbench
Crystal structure of the N-terminal EFC/F-bar domain of SYP1
Analyse Crystal structure of the N-terminal EFC/F-bar domain of SYP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G9G
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Suppressor of yeast profilin deletion
- UniProt
- P25623
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Suppressor of yeast profilin deletion | protein | 250 | 82% helix, 0% strand | P25623 |
Compared structures
- 3G9G · Crystal Structure of the N-terminal EFC/F-BAR domain of Syp1 · the same entry in another collection · chain A against A, TM-score 1.00
- P25623 · AlphaFold monomer V2.0 prediction for suppressor of yeast profilin deletion (P25623) · 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 P25623
- Elsewhere: RCSB PDB 3G9G · PDBe 3G9G · UniProt P25623
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