MolNFT v1 · #152928 · protein
Structure of human RAS-related protein RAB11
6IY1 · RAS-related protein rab-11A: “Structure of human RAS-related protein RAB11”. X-ray diffraction, 1 ligand (GDP), 20 pockets (best druggability 0.73). MolNFT v1 #152928 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IY1
- Type
- protein
- Length
- 988 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein rab-11A
- UniProt
- P62491
- Ligands
- GDP
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | RAS-related protein rab-11A | protein | 165 | 35% helix, 28% strand | P62491 |
| D | RAS-related protein rab-11A | protein | 164 | 38% helix, 29% strand | P62491 |
| E | RAS-related protein rab-11A | protein | 163 | 38% helix, 28% strand | P62491 |
| F | RAS-related protein rab-11A | protein | 166 | 37% helix, 29% strand | P62491 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1036 | 0.73 | 0.76 | 70 | empty |
| 2 | 989 | 0.73 | 0.76 | 80 | empty |
| 3 | 57 | 0.66 | 0.95 | 23 | empty |
| 4 | 61 | 0.66 | 0.94 | 27 | empty |
| 5 | 255 | 0.57 | 0.78 | 28 | empty |
Interfaces
9 interfaces between chains.
- B–D · 1066 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 841 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 841 Ų buried · 14 hydrogen bonds · protein-protein
- D–F · 763 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 356 Ų buried · 1 hydrogen bond · 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 P62491
- Elsewhere: RCSB PDB 6IY1 · PDBe 6IY1 · UniProt P62491
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