Research workbench
The structure of human FMNL1 N-terminal domains bound to CDC42
Analyse The structure of human FMNL1 N-terminal domains bound to CDC42 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YDH
- Type
- protein
- Length
- 1,014 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95466, P60953
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | O95466 |
| B, D | — | protein | 178 | — | P60953 |
| C | — | protein | 328 | — | O95466 |
Compared structures
- 4YDH · The structure of human FMNL1 N-terminal domains bound to Cdc42 · the same entry in another collection · chain D against D, TM-score 1.00
- P60953 · AlphaFold monomer V2.0 prediction for cell division control protein 42 homolog (P60953) · a predicted model of the same protein · chain B against A, TM-score 0.98
- O95466 · AlphaFold monomer V2.0 prediction for formin-like protein 1 (O95466) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 O95466
- Every structure of UniProt P60953
- Elsewhere: RCSB PDB 4YDH · PDBe 4YDH · UniProt O95466 · UniProt P60953
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