Research workbench
Structure of human ARL1 in complex with the dcb domain of BIG1
Analyse Structure of human ARL1 in complex with the dcb domain of BIG1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EE5
- Type
- protein
- Length
- 366 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y6D6, P40616
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 202 | — | Q9Y6D6 |
| B | — | protein | 164 | — | P40616 |
Compared structures
- P40616 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-like protein 1 (P40616) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q9Y6D6 · AlphaFold monomer V2.0 prediction for brefeldin a-inhibited guanine nucleotide-exchange… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9Y6D6
- Every structure of UniProt P40616
- Elsewhere: RCSB PDB 5EE5 · PDBe 5EE5 · UniProt Q9Y6D6 · UniProt P40616
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