Research workbench
Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase
Analyse Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QNK
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-hydroxyanthranilate 3,4-dioxygenase
- EC
- 1.13.11.6
- UniProt
- P46952
- Ligands
- NI, PO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) | protein | 286 | 16% helix, 42% strand | P46952 |
Ligands and binding sites
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 | 269 | 0.71 | 0.85 | 37 | empty |
| 2 | 52 | 0.29 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 2QNK · Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase · the same entry in another collection · chain A against A, TM-score 1.00
- P46952 · AlphaFold monomer V2.0 prediction for 3-hydroxyanthranilate 3,4-dioxygenase (P46952) · 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 P46952
- Elsewhere: RCSB PDB 2QNK · PDBe 2QNK · UniProt P46952
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