Structure of PDB 5zzq Chain A Binding Site BS02

Receptor Information
>5zzq Chain A (length=355) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHT
AREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNH
GGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASA
VLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNT
KLGVV
Ligand information
Ligand IDHHH
InChIInChI=1S/C8H8O4/c9-6-3-1-5(2-4-6)7(10)8(11)12/h1-4,7,9-10H,(H,11,12)/t7-/m0/s1
InChIKeyYHXHKYRQLYQUIH-ZETCQYMHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@H](C(O)=O)c1ccc(O)cc1
ACDLabs 10.04O=C(O)C(O)c1ccc(O)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1C(C(=O)O)O)O
OpenEye OEToolkits 1.5.0c1cc(ccc1[C@@H](C(=O)O)O)O
CACTVS 3.341O[CH](C(O)=O)c1ccc(O)cc1
FormulaC8 H8 O4
Name(2S)-hydroxy(4-hydroxyphenyl)ethanoic acid
ChEMBL
DrugBankDB07896
ZINCZINC000000388426
PDB chain5zzq 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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PDB5zzq Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
Resolution1.32 Å
Binding residue
(original residue number in PDB)		L108 Y128 M160 R163 T202 F206 H252 R255
Binding residue
(residue number reindexed from 1)		L106 Y126 M158 R161 T200 F204 H250 R253
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) Y128 D156 H252
Catalytic site (residue number reindexed from 1) Y126 D154 H250
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
View graph for
Biological Process
External links
PDB RCSB:5zzq, PDBe:5zzq, PDBj:5zzq
PDBsum5zzq
PubMed31373572
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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