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Crystal structure of mouse RABL3 in complex with GDP
Analyse Crystal structure of mouse RABL3 in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VIJ
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rab-like protein 3
- UniProt
- Q9D4V7
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Rab-like protein 3 | protein | 191 | 40% helix, 23% strand | Q9D4V7 |
| A | Rab-like protein 3 | protein | 186 | 42% helix, 23% strand | Q9D4V7 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains B, A
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 | 753 | 0.72 | 0.78 | 79 | MG |
| 2 | 62 | 0.31 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- B–A · 831 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q9D4V7
- Elsewhere: RCSB PDB 6VIJ · PDBe 6VIJ · UniProt Q9D4V7
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