Structure of PDB 1b9i Chain A

Receptor sequence
>1b9iA (length=384) Species: 33910 (Amycolatopsis mediterranei) [Search protein sequence]
KAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAA
HALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVP
VDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGV
PLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGE
TEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDE
QIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEER
RNALVDRLVEAGLPAFAAFRAIYRTDAFWELGAPDESVDAIARRCPNTDA
ISSDCVWLHHRVLLAGEPELHATAEIIADAVGRA
3D structure
PDB1b9i Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase.
ChainA
Resolution2.0 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 PXG A N61 G62 T63 F88 S90 D159 A161 H162 S183 Q185 K188 N57 G58 T59 F84 S86 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1b9i, PDBe:1b9i, PDBj:1b9i
PDBsum1b9i
PubMed10433690
UniProtO52552|RIFK_AMYMS 3-amino-5-hydroxybenzoate synthase (Gene Name=rifK)

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