Structure of PDB 6a0g Chain A Binding Site BS02

Receptor Information
>6a0g Chain A (length=331) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDLP
VVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAV
SGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQL
LELLAEEVRDAMGLAGCESVGAARRLNTKLG
Ligand information
Ligand IDHFA
InChIInChI=1S/C9H10O3/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8,10H,6H2,(H,11,12)/t8-/m0/s1
InChIKeyVOXXWSYKYCBWHO-QMMMGPOBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)CC(C(=O)O)O
OpenEye OEToolkits 1.5.0c1ccc(cc1)C[C@@H](C(=O)O)O
ACDLabs 10.04O=C(O)C(O)Cc1ccccc1
CACTVS 3.341O[C@@H](Cc1ccccc1)C(O)=O
CACTVS 3.341O[CH](Cc1ccccc1)C(O)=O
FormulaC9 H10 O3
NameALPHA-HYDROXY-BETA-PHENYL-PROPIONIC ACID
ChEMBL
DrugBankDB02494
ZINCZINC000000388089
PDB chain6a0g Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6a0g Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		F24 L108 M160 H252 R255
Binding residue
(residue number reindexed from 1)		F22 L106 M158 H228 R231
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F128 D156 H252
Catalytic site (residue number reindexed from 1) F126 D154 H228
Enzyme Commision number 1.1.3.46: 4-hydroxymandelate oxidase.
Gene Ontology
Molecular Function
GO:0004459 L-lactate dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0033072 vancomycin biosynthetic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:6a0g, PDBe:6a0g, PDBj:6a0g
PDBsum6a0g
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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