Research workbench
Hmiro ef hand and cgtpase domains in the gmppcp-bound state
Analyse Hmiro ef hand and cgtpase domains in the gmppcp-bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KSZ
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial rho GTPase 1
- EC
- 3.6.5.-
- UniProt
- Q8IXI2
- Ligands
- GCP, MG, CL
- Pockets
- 10 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial rho GTPase 1 (EC 3.6.5.-) | protein | 398 | 43% helix, 15% strand | Q8IXI2 |
Ligands and binding sites
- GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.70 | 0.88 | 20 | empty |
| 2 | 102 | 0.65 | 0.90 | 16 | empty |
| 3 | 218 | 0.54 | 0.78 | 30 | GCP |
| 4 | 167 | 0.50 | 0.77 | 27 | empty |
| 5 | 172 | 0.46 | 0.75 | 27 | empty |
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 Q8IXI2
- Elsewhere: RCSB PDB 5KSZ · PDBe 5KSZ · UniProt Q8IXI2
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