BioLiP

Structure of PDB 1b9h Chain A

Receptor sequence

>1b9hA (length=384) Species: 33910 (Amycolatopsis mediterranei) [Search protein sequence]

KAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAA
HALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVP
VDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGV
PLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGE
TEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDE
QIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEER
RNALVDRLVEAGLPAFAAFRAIYRTDAFWELGAPDESVDAIARRCPNTDA
ISSDCVWLHHRVLLAGEPELHATAEIIADAVARA

3D structure

PDB

1b9h Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase.

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	F88 D159 H162 Q185 K188 R219 Y226 R236
Catalytic site (residue number reindexed from 1)	F84 D155 H158 Q181 K184 R215 Y222 R232
Enzyme Commision number	2.6.1.- 4.2.1.144: 3-amino-5-hydroxybenzoate synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PLP	A	N61 G62 T63 F88 D159 A161 H162 S183 Q185 K188	N57 G58 T59 F84 D155 A157 H158 S179 Q181 K184

Gene Ontology

	Molecular Function
GO:0008483	transaminase activity
GO:0016740	transferase activity
GO:0016829	lyase activity
GO:0030170	pyridoxal phosphate binding

	Biological Process
GO:0000271	polysaccharide biosynthetic process
GO:0017000	antibiotic biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:1b9h, PDBe:1b9h, PDBj:1b9h
PDBsum	1b9h
PubMed	10433690
UniProt	O52552\|RIFK_AMYMS 3-amino-5-hydroxybenzoate synthase (Gene Name=rifK)