Research workbench
Structure of FE2-hppd bound to ntbc
Analyse Structure of FE2-hppd bound to ntbc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T47
- Type
- protein
- Length
- 724 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxyphenylpyruvate dioxygenase
- EC
- 1.13.11.27
- UniProt
- Q53586
- Ligands
- NTD, FE2
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) | protein | 362 | 29% helix, 34% strand | Q53586 |
Ligands and binding sites
- NTD · 2-{hydroxy[2-nitro-4-(trifluoromethyl) phenyl]methylene}cyclohexane-1,3-dione · ligand · 2 copies · chains A, B
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.75 | 0.80 | 93 | FE2, NTD |
| 2 | 528 | 0.75 | 0.82 | 68 | NTD |
| 3 | 200 | 0.68 | 0.86 | 44 | empty |
| 4 | 254 | 0.61 | 0.80 | 28 | empty |
| 5 | 242 | 0.60 | 0.80 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1346 Ų buried · 20 hydrogen bonds · protein-protein
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 Q53586
- Elsewhere: RCSB PDB 1T47 · PDBe 1T47 · UniProt Q53586
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.