Structure of PDB 1nrg Chain A Binding Site BS02

Receptor Information
>1nrg Chain A (length=213) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLL
LKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKK
LPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQ
EVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTH
RGEEDWLYERLAP
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 chain1nrg Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1nrg Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		R95 M96 L97 L98 F110 T111 S115 R116 K117 Q174 S175
Binding residue
(residue number reindexed from 1)		R47 M48 L49 L50 F62 T63 S67 R68 K69 Q126 S127
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R225
Catalytic site (residue number reindexed from 1) R177
Enzyme Commision number 1.4.3.5: pyridoxal 5'-phosphate synthase.
Gene Ontology
Molecular Function
GO:0004733 pyridoxamine phosphate oxidase activity
GO:0005515 protein binding
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0008615 pyridoxine biosynthetic process
GO:0042816 vitamin B6 metabolic process
GO:0042818 pyridoxamine metabolic process
GO:0042822 pyridoxal phosphate metabolic process
GO:0042823 pyridoxal phosphate biosynthetic process
GO:1901615 organic hydroxy compound metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nrg, PDBe:1nrg, PDBj:1nrg
PDBsum1nrg
PubMed12824491
UniProtQ9NVS9|PNPO_HUMAN Pyridoxine-5'-phosphate oxidase (Gene Name=PNPO)

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