MolNFT v1 · #136731 · protein
1.78 ångström crystal structure of P97H 3-hydroxyanthranilate-3,4- dioxygenase from cupriavidus metallidurans
5V26 · 3-hydroxyanthranilate 3,4-dioxygenase: “1.78 ångström crystal structure of P97H 3-hydroxyanthranilate-3,4- dioxygenase from cupriavidus metallidurans”. X-ray diffraction, 1 ligand (FE2), 2 pockets (best druggability 0.82). MolNFT v1…
- PDB
- 5V26
- Type
- protein
- Length
- 343 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-hydroxyanthranilate 3,4-dioxygenase
- EC
- 1.13.11.6
- UniProt
- Q1LCS4
- Ligands
- FE2
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) | protein | 171 | 15% helix, 38% strand | Q1LCS4 |
| B | 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) | protein | 172 | 14% helix, 38% strand | Q1LCS4 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.82 | 0.84 | 79 | FE2 |
| 2 | 53 | 0.34 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5V26 · 1.78 angstrom crystal structure of P97H 3-hydroxyanthranilate-3,4-dioxygenase from… · 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 0.97
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 5V26 · PDBe 5V26 · UniProt Q1LCS4
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