Research workbench
P-hydroxybenzoate hydroxylase (phbh) mutant with cys 116 replaced by ser (C116S) and his 162 replaced by arg (H162R), in complex with FAD and 4-hydroxybenzoic acid
Analyse P-hydroxybenzoate hydroxylase (phbh) mutant with cys 116 replaced by ser… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BGJ
- Type
- protein
- Length
- 391 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P-hydroxybenzoate hydroxylase
- EC
- 1.14.13.2
- UniProt
- P00438
- Ligands
- FAD, PHB
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P-hydroxybenzoate hydroxylase (EC 1.14.13.2) | protein | 391 | 40% helix, 28% strand | P00438 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- PHB · P-hydroxybenzoic acid · ligand · 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 | 634 | 0.77 | 0.83 | 63 | FAD, PHB |
| 2 | 112 | 0.40 | 0.76 | 18 | empty |
Compared structures
- 1BGJ · P-hydroxybenzoate hydroxylase (phbh) mutant with cys 116 replaced by ser (C116S) and his… · the same entry in another collection · chain A against A, TM-score 1.00
- P00438 · AlphaFold monomer V2.0 prediction for P-hydroxybenzoate hydroxylase (P00438) · a predicted model of the same protein · 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 P00438
- Elsewhere: RCSB PDB 1BGJ · PDBe 1BGJ · UniProt P00438
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