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1R53

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004107molecular_functionchorismate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008752molecular_functionFMN reductase (NAD(P)H) activity
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0042602molecular_functionriboflavin reductase (NADPH) activity
A0052873molecular_functionFMN reductase (NADPH) activity
Functional Information from PROSITE/UniProt
site_idPS00787
Number of Residues16
DetailsCHORISMATE_SYNTHASE_1 Chorismate synthase signature 1. GESHCksVGcIVDGvP
ChainResidueDetails
AGLY14-PRO29

site_idPS00788
Number of Residues17
DetailsCHORISMATE_SYNTHASE_2 Chorismate synthase signature 2. GraSAReTigrVasGAI
ChainResidueDetails
AGLY122-ILE138

site_idPS00789
Number of Residues17
DetailsCHORISMATE_SYNTHASE_3 Chorismate synthase signature 3. RHDPAvtprAiPIvEAM
ChainResidueDetails
AARG337-MET353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q12640
ChainResidueDetails
AHIS17
AHIS104
AASP339

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2

227111

PDB entries from 2024-11-06

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