Research workbench
Crystal structure of the efc domain of CDC42-interacting protein 4
Analyse Crystal structure of the efc domain of CDC42-interacting protein 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EFK
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CDC42-interacting protein 4
- UniProt
- Q15642
Structure
x-ray diffraction · 1 distinct chain · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CDC42-interacting protein 4 | protein | 273 | 89% helix, 0% strand | Q15642 |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2EFK · Crystal structure of the EFC domain of Cdc42-interacting protein 4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q15642 · AlphaFold monomer V2.0 prediction for CDC42-interacting protein 4 (Q15642) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q15642
- Elsewhere: RCSB PDB 2EFK · PDBe 2EFK · UniProt Q15642
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