Structure of PDB 6a0d Chain A Binding Site BS02

Receptor Information
>6a0d Chain A (length=327) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDL
TDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTI
CTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTV
DVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPVVLK
GILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGC
EVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELL
AEEVRDAMGLAGCESVGAARRLNTKLG
Ligand information
Ligand ID9RW
InChIInChI=1S/C9H10O2/c1-7(9(10)11)8-5-3-2-4-6-8/h2-7H,1H3,(H,10,11)/t7-/m0/s1
InChIKeyYPGCWEMNNLXISK-ZETCQYMHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CC(c1ccccc1)C(=O)O
OpenEye OEToolkits 2.0.6C[C@@H](c1ccccc1)C(=O)O
CACTVS 3.385C[CH](C(O)=O)c1ccccc1
CACTVS 3.385C[C@H](C(O)=O)c1ccccc1
FormulaC9 H10 O2
Name(2~{S})-2-phenylpropanoic acid
ChEMBL
DrugBank
ZINCZINC000000391877
PDB chain6a0d 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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PDB6a0d Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
Resolution1.65 Å
Binding residue
(original residue number in PDB)		F24 M160 R163 H252 R255
Binding residue
(residue number reindexed from 1)		F19 M155 R158 H224 R227
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F128 D156 H252
Catalytic site (residue number reindexed from 1) F123 D151 H224
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6a0d, PDBe:6a0d, PDBj:6a0d
PDBsum6a0d
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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