Structure of PDB 6a24 Chain A Binding Site BS01

Receptor Information
>6a24 Chain A (length=354) 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
KLGV
Ligand information
Ligand IDFMN
InChIInChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
InChIKeyFVTCRASFADXXNN-SCRDCRAPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)O)O)O)O
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
ACDLabs 12.01N=2C(=O)NC(=O)C3=Nc1cc(C)c(C)cc1N(C=23)CC(O)C(O)C(O)COP(=O)(O)O
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
FormulaC17 H21 N4 O9 P
NameFLAVIN MONONUCLEOTIDE;
RIBOFLAVIN MONOPHOSPHATE
ChEMBLCHEMBL1201794
DrugBankDB03247
ZINCZINC000003831425
PDB chain6a24 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6a24 Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Resolution1.39 Å
Binding residue
(original residue number in PDB)		P77 V78 A79 Q126 Y128 T154 K228 H252 G253 R255 D283 G284 G285 R287 G306 R307
Binding residue
(residue number reindexed from 1)		P75 V76 A77 Q124 Y126 T152 K226 H250 G251 R253 D281 G282 G283 R285 G304 R305
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6a24, PDBe:6a24, PDBj:6a24
PDBsum6a24
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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