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Receptor Information

>6a3d Chain A (length=327) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLT
DVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTIC
TLSSVSLEEIAAVGGRPWFQLFWLRDEKRSLDLVRRAEDAGCEAIVFTVD
VPWMGRRLRDMRNGFALPEVTAANFDFAPATWESVEAVRAHTDLPVVLKG
ILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCE
VLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLA
EEVRDAMGLAGCESVGAARRLNTKLGV

Ligand ID

9PX

InChI

InChI=1S/C19H25N4O13P/c1-8-4-10-11(5-9(8)2)23(6-12(24)14(26)13(25)7-34-37(30,31)32)15-19(22-10,36-35-18(29)33-3)16(27)21-17(28)20-15/h4-5,12-14,22,24-26H,6-7H2,1-3H3,(H,21,27,28)(H2,30,31,32)/t12-,13+,14-,19-/m0/s1

InChIKey

BKTAMFVARSDVLC-LJPSSGMGSA-N

SMILES

Software	SMILES
CACTVS 3.385	COC(=O)OO[C@@]12Nc3cc(C)c(C)cc3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)C1=NC(=O)NC2=O
ACDLabs 12.01	Cc1cc3c(cc1C)N(C=2C(C(=O)NC(N=2)=O)(N3)OOC(=O)OC)CC(C(C(O)COP(O)(=O)O)O)O
OpenEye OEToolkits 2.0.6	Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)[C@@]3(N2)OOC(=O)OC)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
OpenEye OEToolkits 2.0.6	Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3(N2)OOC(=O)OC)CC(C(C(COP(=O)(O)O)O)O)O
CACTVS 3.385	COC(=O)OO[C]12Nc3cc(C)c(C)cc3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)C1=NC(=O)NC2=O

Formula

C19 H25 N4 O13 P

Name

1-deoxy-1-[(4aS)-4a-[(methoxycarbonyl)peroxy]-7,8-dimethyl-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-5-O-phosphono-D-ribitol

ChEMBL

DrugBank

ZINC

PDB chain

6a3d 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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Structure summary

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PDB	6a3d Structural and chemical trapping of flavin-oxide intermediates reveals substrate-directed reaction multiplicity.
Resolution	1.923 Å
Binding residue (original residue number in PDB)	P77 V78 A79 F128 T154 K228 H252 R255 D283 G284 G285 R287 G306 R307
Binding residue (residue number reindexed from 1)	P71 V72 A73 F122 T148 K199 H223 R226 D254 G255 G256 R258 G277 R278
Annotation score	1

Catalytic site (original residue number in PDB)	F128 D156 H252
Catalytic site (residue number reindexed from 1)	F122 D150 H223
Enzyme Commision number	1.1.3.46: 4-hydroxymandelate oxidase.

	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

PDB	RCSB:6a3d, PDBe:6a3d, PDBj:6a3d
PDBsum	6a3d
PubMed	32362037
UniProt	O52792\|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)

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Structure of PDB 6a3d Chain A Binding Site BS01