Structure of PDB 6a1w Chain A Binding Site BS02

Receptor Information
>6a1w Chain A (length=334) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRM
LRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGV
PYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAI
VFTVDVPWMGRRLRDMRNGFALPEWVTAANFDFAPATWESVEAVRAHTDL
PVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAA
VSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQ
LLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV
Ligand information
Ligand ID9P3
InChIInChI=1S/C19H23N4O11P/c1-8-4-11-12(5-9(8)2)23(10(3)24)19(34-23)16(20-18(29)21-17(19)28)22(11)6-13(25)15(27)14(26)7-33-35(30,31)32/h4-5,13-15,25-27H,6-7H2,1-3H3,(H2-,21,28,29,30,31,32)/p+1/t13-,14+,15-,19+,23+/m0/s1
InChIKeyCNQDYQZVEZBXRL-PIOSDFFKSA-O
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)[N@+]12O[C@]13C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c4cc(C)c(C)cc24
ACDLabs 12.01C2=4N(c1cc(C)c(C)cc1[N+]3(C2(O3)C(=O)NC(N=4)=O)C(C)=O)CC(C(C(O)COP(O)(O)=O)O)O
CACTVS 3.385CC(=O)[N+]12O[C]13C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c4cc(C)c(C)cc24
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)[N+]3(C4(O3)C(=O)NC(=O)N=C4N2CC(C(C(COP(=O)(O)O)O)O)O)C(=O)C
OpenEye OEToolkits 2.0.6Cc1cc2c(cc1C)[N@@+]3([C@]4(O3)C(=O)NC(=O)N=C4N2C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)C(=O)C
FormulaC19 H24 N4 O11 P
Name1-[(1aR,11R)-11-acetyl-8,9-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]oxazireno[3,2-e]pteridin-11-ium-6(2H)-yl]-1-deoxy-5-O-phosphono-D-ribitol
ChEMBL
DrugBank
ZINC
PDB chain6a1w Chain A Residue 402 [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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PDB6a1w Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		L25 A76 P77 V78 Q126 Y128 T154 R163 K228 H252 R255 D283 G285 R287 G306 R307
Binding residue
(residue number reindexed from 1)		L24 A75 P76 V77 Q125 Y127 T153 R162 K205 H229 R232 D260 G262 R264 G283 R284
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y128 D156 H252
Catalytic site (residue number reindexed from 1) Y127 D155 H229
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:6a1w, PDBe:6a1w, PDBj:6a1w
PDBsum6a1w
PubMed32362037
UniProtO52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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