Research workbench
Crystal structure of acanthamoeba polyphaga mimivirus rab GTPase in complex with GTP
Analyse Crystal structure of acanthamoeba polyphaga mimivirus rab GTPase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XC5
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable rab-related GTPase
- UniProt
- Q5UQ27
- Ligands
- GTP, MG
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable rab-related GTPase | protein | 167 | 39% helix, 25% strand | Q5UQ27 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.35 | 0.78 | 17 | GTP, MG |
Compared structures
- 5XC5 · Crystal structure of Acanthamoeba polyphaga mimivirus Rab GTPase in complex with GTP · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5UQ27
- Elsewhere: RCSB PDB 5XC5 · PDBe 5XC5 · UniProt Q5UQ27
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