MolNFT v1 · #67716 · protein
Crystal structure of human 4-hydroxyphenylpyruvate dioxygenase
3ISQ: “Crystal structure of human 4-hydroxyphenylpyruvate dioxygenase”. X-ray diffraction, 3 ligands (CO, NA, CL), 5 pockets (best druggability 0.76). MolNFT v1 #67716 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3ISQ
- Type
- protein
- Length
- 376 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxyphenylpyruvate dioxygenase
- EC
- 1.13.11.27
- UniProt
- P32754
- Ligands
- CO, NA, CL
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) | protein | 376 | 28% helix, 36% strand | P32754 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · chains A
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · 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 | 70 | 0.76 | 0.99 | 23 | CO |
| 2 | 298 | 0.65 | 0.81 | 28 | EDO |
| 3 | 119 | 0.48 | 0.79 | 23 | empty |
| 4 | 79 | 0.48 | 0.82 | 16 | empty |
| 5 | 94 | 0.36 | 0.74 | 21 | empty |
Compared structures
- 3ISQ · Crystal structure of human 4-Hydroxyphenylpyruvate dioxygenase · the same entry in another collection · chain A against A, TM-score 1.00
- P32754 · AlphaFold monomer V2.0 prediction for 4-hydroxyphenylpyruvate dioxygenase (P32754) · 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 P32754
- Elsewhere: RCSB PDB 3ISQ · PDBe 3ISQ · UniProt P32754
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