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Crystal structure of HPPD complexed with Y18556
Analyse Crystal structure of HPPD complexed with Y18556 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V6X
- Type
- protein
- Length
- 379 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Arabidopsis thaliana
- Molecule
- 4-hydroxyphenylpyruvate dioxygenase
- EC
- 1.13.11.27
- UniProt
- P93836
- Ligands
- 5RJ, CO
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 30% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) | protein | 379 | 30% helix, 34% strand | P93836 |
Ligands and binding sites
- 5RJ · 5-methyl-3-[(2-methylphenyl)methyl]-6-[(1~{R},2~{S})-2-oxidanyl-6-oxidanylidene-cyclohexyl]carbonyl-1,2,3-benzotriazin-4-one · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
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 | 421 | 0.69 | 0.80 | 44 | 5RJ |
| 2 | 67 | 0.34 | 0.76 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P93836
- Elsewhere: RCSB PDB 7V6X · PDBe 7V6X · UniProt P93836
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