MolNFT v2 · #153346 · protein
Complex structure of Rab35 and its effector ACAP2
6IF3: “Complex structure of Rab35 and its effector ACAP2”. X-ray diffraction at 1.5, 2 ligands (GTP, MG). MolNFT v2 #153346 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IF3
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Homo sapiens
- UniProt
- Q15057, Q15286
- Ligands
- GTP, MG
Structure
x-ray diffraction · resolution 1.5 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 159 | — | Q15057 |
| B | — | protein | 177 | — | Q15286 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IF3 · Complex structure of RAB35 and its effector ACAP2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q15286 · AlphaFold monomer V2.0 prediction for RAS-related protein rab-35 (Q15286) · a predicted model of the same protein · chain B against A, TM-score 0.96
- Q15057 · AlphaFold monomer V2.0 prediction for arf-gap with coiled-coil, ank repeat and pH… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q15057
- Every structure of UniProt Q15286
- Elsewhere: RCSB PDB 6IF3 · PDBe 6IF3 · UniProt Q15057 · UniProt Q15286
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