BioLiP

Receptor Information

>1nas Chain A (length=259) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ADGLGCAVCVLTGASRGFGRALAPQLARLLSPGSVMLVSARSESMLRQLK
EELGAQQPDLKVVLAAADLGTEAGVQRLLSAVRELPRPEGLQRLLLINNA
ATLGDVSKGFLNVNDLAEVNNYWALNLTSMLCLTSGTLNAFQDSPGLSKT
VVNISSLCALQPYKGWGLYCAGKAARDMLYQVLAAEEPSVRVLSYAPGPL
DNDMQQLARETSKDPELRSKLQKLKSDGALVDCGTSAQKLLGLLQKDTFQ
SGAHVDFYD

Ligand ID

NAP

InChI

InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

InChIKey

XJLXINKUBYWONI-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N

Formula

C21 H28 N7 O17 P3

Name

NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

PDB chain

1nas Chain A Residue 800 [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	1nas The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters.
Resolution	2.1 Å
Binding residue (original residue number in PDB)	G15 S17 R18 G19 F20 R43 S44 D70 L71 N101 A102 A103 L127 I156 Y171 K175 P199 G200 L202 N204 M206
Binding residue (residue number reindexed from 1)	G13 S15 R16 G17 F18 R41 S42 D68 L69 N99 A100 A101 L125 I154 Y169 K173 P197 G198 L200 N202 M204
Annotation score	4

Enzyme Commision number

1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).

	Molecular Function
GO:0004757	sepiapterin reductase (NADP+) activity
GO:0016491	oxidoreductase activity
GO:0042803	protein homodimerization activity

	Biological Process
GO:0006558	L-phenylalanine metabolic process
GO:0006729	tetrahydrobiopterin biosynthetic process
GO:0019889	pteridine metabolic process
GO:0040014	regulation of multicellular organism growth
GO:0042415	norepinephrine metabolic process
GO:0042417	dopamine metabolic process
GO:0042428	serotonin metabolic process
GO:0046146	tetrahydrobiopterin metabolic process
GO:0048667	cell morphogenesis involved in neuron differentiation
GO:0050882	voluntary musculoskeletal movement

	Cellular Component
GO:0005737	cytoplasm
GO:0005739	mitochondrion

PDB	RCSB:1nas, PDBe:1nas, PDBj:1nas
PDBsum	1nas
PubMed	9405351
UniProt	Q64105\|SPRE_MOUSE Sepiapterin reductase (Gene Name=Spr)

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Structure of PDB 1nas Chain A Binding Site BS02