Structure of PDB 6a1p Chain A Binding Site BS01

Receptor Information
>6a1p Chain A (length=332) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
Ligand information
Ligand ID9O9
InChIInChI=1S/C18H22N3O9P/c1-8-3-10-5-11-16(19-18(26)20-17(11)25)21(12(10)4-9(8)2)6-13(22)15(24)14(23)7-30-31(27,28)29/h3-5,13-15,22-24H,6-7H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t13-,14+,15-/m0/s1
InChIKeyLAWFKZVKVIYTAR-ZNMIVQPWSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01C3(=O)C2=Cc1c(cc(c(C)c1)C)N(C2=NC(N3)=O)CC(C(C(O)COP(O)(O)=O)O)O
CACTVS 3.385Cc1cc2C=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=C2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
CACTVS 3.385Cc1cc2C=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=C2)CC(C(C(COP(=O)(O)O)O)O)O
FormulaC18 H22 N3 O9 P
Name1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phosphono-D-ribitol
ChEMBL
DrugBank
ZINC
PDB chain6a1p 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6a1p The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
Resolution1.51 Å
Binding residue
(original residue number in PDB)		A76 P77 V78 Q126 F128 T154 K228 H252 R255 D283 G285 R287 G306 R307
Binding residue
(residue number reindexed from 1)		A74 P75 V76 Q124 F126 T152 K203 H227 R230 D258 G260 R262 G281 R282
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F128 D156 H252
Catalytic site (residue number reindexed from 1) F126 D154 H227
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:6a1p, PDBe:6a1p, PDBj:6a1p
PDBsum6a1p
PubMed31588923
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

[Back to BioLiP]