Research workbench
Crystal structure analysis of RAC1-GDP in complex with arfaptin (P41)
Analyse Crystal structure analysis of RAC1-GDP in complex with arfaptin (P41) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I4L
- Type
- protein
- Length
- 540 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53365, P63000
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | P53365 |
| B | — | protein | 178 | — | P53365 |
| D | — | protein | 177 | — | P63000 |
Compared structures
- 1I4L · Crystal structure analysis of RAC1-GDP in complex with arfaptin (P41) · the same entry in another collection · chain A against A, TM-score 1.00
- P63000 · AlphaFold monomer V2.0 prediction for RAS-related C3 botulinum toxin substrate 1 (P63000) · a predicted model of the same protein · chain D against A, TM-score 0.96
- P53365 · AlphaFold monomer V2.0 prediction for arfaptin-2 (P53365) · a predicted model of the same protein · chain B 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 P53365
- Every structure of UniProt P63000
- Elsewhere: RCSB PDB 1I4L · PDBe 1I4L · UniProt P53365 · UniProt P63000
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