MolNFT v1 · #87412 · protein
Crystal structure of drosophila miro ef hand and cgtpase domains in the apo state (apo-miros)
4C0J · Mitochondrial rho GTPase: “Crystal structure of drosophila miro ef hand and cgtpase domains in the apo state (apo-miros)”. X-ray diffraction, 4 ligands (HSE, NA, SO4), 9 pockets (best druggability 0.73). MolNFT v1 #87412 on…
- PDB
- 4C0J
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial rho GTPase
- EC
- 3.6.5.-
- UniProt
- Q8IMX7
- Ligands
- HSE, NA, SO4, UNX
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial rho GTPase (EC 3.6.5.-) | protein | 404 | 42% helix, 15% strand | Q8IMX7 |
Ligands and binding sites
- HSE · L-homoserine · ligand · chains A
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- UNX · Unknown atom or ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.73 | 0.87 | 29 | HSE |
| 2 | 179 | 0.48 | 0.76 | 31 | SO4 |
| 3 | 141 | 0.48 | 0.78 | 20 | SO4 |
| 4 | 65 | 0.39 | 0.79 | 14 | empty |
| 5 | 58 | 0.34 | 0.78 | 16 | empty |
Compared structures
- 4C0J · Crystal structure of Drosophila Miro EF hand and cGTPase domains in the apo state… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IMX7 · AlphaFold monomer V2.0 prediction for mitochondrial rho GTPase (Q8IMX7) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8IMX7
- Elsewhere: RCSB PDB 4C0J · PDBe 4C0J · UniProt Q8IMX7
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