MolNFT v2 · #94421 · protein
1.75 angstrom x-ray crystal structure of cufe reconstituted 3-hydroxyanthranilate-3,4-dioxygenase from cupriavidus metallidurans
4HVO · 3-hydroxyanthranilate 3,4-dioxygenase: “1.75 angstrom x-ray crystal structure of cufe reconstituted 3-hydroxyanthranilate-3,4-dioxygenase from…”. X-ray diffraction at 1.75, 2 ligands (CU, FE2), 1 pocket (best druggability 0.73).…
- PDB
- 4HVO
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Cupriavidus metallidurans
- Molecule
- 3-hydroxyanthranilate 3,4-dioxygenase
- EC
- 1.13.11.6
- UniProt
- Q1LCS4
- Ligands
- CU, FE2
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 16% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) | protein | 174 | 16% helix, 37% strand | Q1LCS4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.73 | 0.83 | 46 | empty |
Compared structures
- 4HVO · 1.75 ångström X-ray crystal structure of cufe reconstituted 3… · the same entry in another collection · chain A against A, TM-score 1.00
- Q1LCS4 · AlphaFold monomer V2.0 prediction for 3-hydroxyanthranilate 3,4-dioxygenase (Q1LCS4) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q1LCS4
- Elsewhere: RCSB PDB 4HVO · PDBe 4HVO · UniProt Q1LCS4
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