Research workbench
Complex structure of RAB35 and its effector ACAP2
Analyse Complex structure of RAB35 and its effector ACAP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IF3
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arf-gap with coiled-coil, ank repeat and pH domain- containing protein 2; RAS-related…
- UniProt
- Q15057, Q15286
- Ligands
- GTP, MG
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arf-gap with coiled-coil, ank repeat and pH domain- containing protein 2 | protein | 159 | 52% helix, 1% strand | Q15057 |
| B | RAS-related protein rab-35 | protein | 177 | 37% helix, 28% strand | Q15286 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.57 | 0.79 | 35 | GTP, MG |
| 2 | 80 | 0.42 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 936 Ų buried · 7 hydrogen bonds · protein-protein
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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