Research workbench
High resolution crystal structure of human RAB9 GTPase: a novel antiviral drug target
Analyse High resolution crystal structure of human RAB9 GTPase: a novel antiviral drug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WMS
- Type
- protein
- Length
- 333 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein rab-9A
- UniProt
- P51151
- Ligands
- GDP
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-9A | protein | 170 | 36% helix, 26% strand | P51151 |
| B | RAS-related protein rab-9A | protein | 163 | 37% helix, 26% strand | P51151 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 902 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1WMS · High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target · the same entry in another collection · chain A against A, TM-score 1.00
- P51151 · AlphaFold monomer V2.0 prediction for RAS-related protein rab-9A (P51151) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P51151
- Elsewhere: RCSB PDB 1WMS · PDBe 1WMS · UniProt P51151
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