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Crystal structure of the P-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 ångströms resolution. analysis of the enzyme- substrate and enzyme-product complexes

Analyse Crystal structure of the P-hydroxybenzoate hydroxylase-substrate complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PBE
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 · 41% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P-hydroxybenzoate hydroxylase (EC 1.14.13.2)	protein	391	41% helix, 29% 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	622	0.77	0.83	58	FAD, PHB
2	106	0.43	0.77	18	empty

Compared structures

1PBE · Crystal structure of the P-hydroxybenzoate hydroxylase-substrate complex refined at 1.9… · 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

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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 1PBE · PDBe 1PBE · UniProt P00438

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