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Crystal structure of 3-amino-5-hydroxybenzoic acid (ahba) synthase

Analyse Crystal structure of 3-amino-5-hydroxybenzoic acid (ahba) synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B9I
Type: protein
Length: 384 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (3-amino-5-hydroxybenzoic acid synthase)
UniProt: O52552
Ligands: PXG
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (3-amino-5-hydroxybenzoic acid synthase)	protein	384	44% helix, 15% strand	O52552

Ligands and binding sites

PXG · 3-[O-phosphonopyridoxyl]--amino-benzoic acid · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	104	0.51	0.82	28	PXG

Compared structures

1B9I · Crystal structure of 3-amino-5-hydroxybenzoic acid (ahba) synthase · the same entry in another collection · chain A against A, TM-score 1.00
O52552 · AlphaFold monomer V2.0 prediction for 3-amino-5-hydroxybenzoate synthase (O52552) · 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 O52552
Elsewhere: RCSB PDB 1B9I · PDBe 1B9I · UniProt O52552

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