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Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4- hydroxyphenylpyruvate dioxygenases
Analyse Structural basis for herbicidal inhibitor selectivity revealed by comparison of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TFZ
- Type
- protein
- Length
- 364 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
- P93836
- Ligands
- 869, FE
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 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 | 364 | 30% helix, 34% strand | P93836 |
Ligands and binding sites
- 869 · (1-tert-butyl-5-hydroxy-1H-pyrazol-4-yl)[6-(methylsulfonyl)-4'-methoxy-2-methyl-1,1'-biphenyl-3-yl]methanone · ligand · chains A
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 412 | 0.67 | 0.79 | 40 | FE, 869 |
| 2 | 71 | 0.39 | 0.78 | 15 | empty |
| 3 | 61 | 0.32 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1TFZ · Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal… · the same entry in another collection · chain A against A, TM-score 1.00
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 1TFZ · PDBe 1TFZ · UniProt P93836
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