MolNFT v1 · #142985 · protein
Vioc L-arginine hydroxylase bound to the vanadyl ion, L-arginine, and succinate
6ALR · Alpha-ketoglutarate-dependent L-arginine hydroxylase: “Vioc L-arginine hydroxylase bound to the vanadyl ion, L-arginine, and succinate”. X-ray diffraction, 2 ligands (ARG, VVO), 5 pockets (best druggability 0.66). MolNFT v1 #142985…
- PDB
- 6ALR
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-ketoglutarate-dependent L-arginine hydroxylase
- EC
- 1.14.11.41
- UniProt
- Q6WZB0
- Ligands
- ARG, VVO
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent L-arginine hydroxylase (EC 1.14.11.41) | protein | 337 | 34% helix, 22% strand | Q6WZB0 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
- VVO · oxovanadium(2+) · ligand · chains A
- SIN · Succinic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.66 | 0.96 | 18 | ARG, VVO |
| 2 | 171 | 0.57 | 0.81 | 23 | empty |
| 3 | 55 | 0.44 | 0.84 | 22 | empty |
| 4 | 58 | 0.35 | 0.78 | 14 | empty |
| 5 | 69 | 0.31 | 0.74 | 15 | empty |
Compared structures
- 6ALR · VioC L-arginine hydroxylase bound to the vanadyl ion, L-arginine, and succinate · the same entry in another collection · chain A against A, TM-score 1.00
- Q6WZB0 · AlphaFold monomer V2.0 prediction for alpha-ketoglutarate-dependent L-arginine… · a predicted model of the same protein · 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 Q6WZB0
- Elsewhere: RCSB PDB 6ALR · PDBe 6ALR · UniProt Q6WZB0
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