Structure of PDB 6a36 Chain A Binding Site BS01

Receptor Information
>6a36 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
FTVDVPWMGRRLRDMRNGFALPEWVTAANFEFAPATWESVEAVRAHTDLP
VVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAV
SGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQL
LELLAEEVRDAMGLAGCESVGAARRLNTKLG
Ligand information
Ligand ID9P9
InChIInChI=1S/C22H28FN4O13P/c1-9-3-11-12(4-10(9)2)27(15(30)5-22(36,8-23)20(33)34)16-18(24-21(35)25-19(16)32)26(11)6-13(28)17(31)14(29)7-40-41(37,38)39/h3-4,13-14,17,28-29,31,36H,5-8H2,1-2H3,(H,33,34)(H2,37,38,39)(H2,24,25,32,35)/t13-,14+,17-,22+/m0/s1
InChIKeyOPWYTCBSKCFWKS-TYGMBGIGSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1cc2N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)C3=C(N(C(=O)C[C@@](O)(CF)C(O)=O)c2cc1C)C(=O)NC(=O)N3
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)N(C3=C(N2CC(C(C(COP(=O)(O)O)O)O)O)NC(=O)NC3=O)C(=O)CC(CF)(C(=O)O)O
CACTVS 3.385Cc1cc2N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)C3=C(N(C(=O)C[C](O)(CF)C(O)=O)c2cc1C)C(=O)NC(=O)N3
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)N(C3=C(N2C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)NC(=O)NC3=O)C(=O)C[C@@](CF)(C(=O)O)O
ACDLabs 12.01OP(=O)(O)OCC(O)C(C(CN2c1cc(C)c(C)cc1N(C(=O)CC(C(O)=O)(O)CF)C3=C2NC(NC3=O)=O)O)O
FormulaC22 H28 F N4 O13 P
Name1-{5-[(3S)-3-carboxy-4-fluoro-3-hydroxybutanoyl]-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl}-1-deoxy-5-O-phosphono-D-ribitol
ChEMBL
DrugBank
ZINC
PDB chain6a36 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6a36 Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Resolution1.44 Å
Binding residue
(original residue number in PDB)		L25 P77 V78 A79 Q126 F128 T154 M160 R163 K228 H252 R255 D283 G284 G285 R287 G306 R307
Binding residue
(residue number reindexed from 1)		L23 P75 V76 A77 Q124 F126 T152 M158 R161 K204 H228 R231 D259 G260 G261 R263 G282 R283
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
View graph for
Biological Process
External links
PDB RCSB:6a36, PDBe:6a36, PDBj:6a36
PDBsum6a36
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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