Research workbench
Crystal structure of human 3HAO with iron bound in the active site
Analyse Crystal structure of human 3HAO with iron bound in the active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TK5
- Type
- protein
- Length
- 283 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
- FE, SO4
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) | protein | 283 | 17% helix, 41% strand | P46952 |
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 | 347 | 0.69 | 0.82 | 59 | empty |
Compared structures
- 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 5TK5 · PDBe 5TK5 · UniProt P46952
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