Structure of PDB 1sep Chain A

Receptor sequence
>1sepA (length=259) Species: 10090 (Mus musculus) [Search protein sequence]
ADGLGCAVCVLTGASRGFGRALAPQLARLLSPGSVMLVSARSESMLRQLK
EELGAQQPDLKVVLAAADLGTEAGVQRLLSAVRELPRPEGLQRLLLINNA
ATLGDVSKGFLNVNDLAEVNNYWALNLTSMLCLTSGTLNAFQDSPGLSKT
VVNISSLCALQPYKGWGLYCAGKAARDMLYQVLAAEEPSVRVLSYAPGPL
DNDMQQLARETSKDPELRSKLQKLKSDGALVDCGTSAQKLLGLLQKDTFQ
SGAHVDFYD
3D structure
PDB1sep The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters.
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).
Interaction with ligand
Gene Ontology
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1sep, PDBe:1sep, PDBj:1sep
PDBsum1sep
PubMed9405351
UniProtQ64105|SPRE_MOUSE Sepiapterin reductase (Gene Name=Spr)

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