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Information on 1dia
PDB: 1dia
Compound: methylenetetrahydrofolate dehydrogenaseCYCLOHYDROL
Classification: OXIDOREDUCTASE,HYDROLASE
Entry date in PDB: 2000-07-05
Resolution [Å]: 2.20
R-Factor: 0.227


CHAIN: A
SWISS-PROT/TREMBL: P11586
   KEYWORD: 3D-structure    Amino-acid biosynthesis    ATP-binding    Disease mutation    Histidine biosynthesis    Hydrolase    Ligase    Methionine biosynthesis    Multifunctional enzyme    NADP    One-carbon metabolism    Oxidoreductase    Polymorphism    Purine biosynthesis   
EC: 1.5.1.5
SCOP: c.2.1.7 Alpha and beta proteins (a/b)    NAD(P)-binding Rossmann-fold domains    NAD(P)-binding Rossmann-fold domains    Aminoacid dehydrogenase-like, C-terminal domain    Methylenetetrahydrofolate dehydrogenase/cyclohydrolase    Human (Homo sapiens)
SCOP: c.58.1.2 Alpha and beta proteins (a/b)    Aminoacid dehydrogenase-like, N-terminal domain    Aminoacid dehydrogenase-like, N-terminal domain    Tetrahydrofolate dehydrogenase/cyclohydrolase    Tetrahydrofolate dehydrogenase/cyclohydrolase    Human (Homo sapiens)
GO:  ATP binding    catalytic activity    formate-tetrahydrofolate ligase activity    folic acid and derivative biosynthesis   


CHAIN: B
SWISS-PROT/TREMBL: P11586
   KEYWORD: 3D-structure    Amino-acid biosynthesis    ATP-binding    Disease mutation    Histidine biosynthesis    Hydrolase    Ligase    Methionine biosynthesis    Multifunctional enzyme    NADP    One-carbon metabolism    Oxidoreductase    Polymorphism    Purine biosynthesis   
EC: 1.5.1.5
SCOP: c.2.1.7 Alpha and beta proteins (a/b)    NAD(P)-binding Rossmann-fold domains    NAD(P)-binding Rossmann-fold domains    Aminoacid dehydrogenase-like, C-terminal domain    Methylenetetrahydrofolate dehydrogenase/cyclohydrolase    Human (Homo sapiens)
SCOP: c.58.1.2 Alpha and beta proteins (a/b)    Aminoacid dehydrogenase-like, N-terminal domain    Aminoacid dehydrogenase-like, N-terminal domain    Tetrahydrofolate dehydrogenase/cyclohydrolase    Tetrahydrofolate dehydrogenase/cyclohydrolase    Human (Homo sapiens)
GO:  ATP binding    catalytic activity    formate-tetrahydrofolate ligase activity    folic acid and derivative biosynthesis   
1dia Image
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Homologous structures to 1dia classified in ArchDB

1a4i A - percentage of sequence identity: 100