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
PDB1b9h Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
External links
PDB RCSB:1b9h, PDBe:1b9h, PDBj:1b9h
PDBsum1b9h
PubMed10433690
UniProtO52552|RIFK_AMYMS 3-amino-5-hydroxybenzoate synthase (Gene Name=rifK)

[Back to BioLiP]