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4ECD

2.5 Angstrom Resolution Crystal Structure of Bifidobacterium longum Chorismate Synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004107molecular_functionchorismate synthase activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0010181molecular_functionFMN binding
A0016829molecular_functionlyase activity
B0004107molecular_functionchorismate synthase activity
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0010181molecular_functionFMN binding
B0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
ASER375
AVAL376
AALA377

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AGLY171
AGLY221
AHOH554

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 402
ChainResidue
BGLY171
BHOH501

Functional Information from PROSITE/UniProt
site_idPS00787
Number of Residues16
DetailsCHORISMATE_SYNTHASE_1 Chorismate synthase signature 1. GESHGeaLVaMIEGlP
ChainResidueDetails
AGLY8-PRO23

site_idPS00789
Number of Residues17
DetailsCHORISMATE_SYNTHASE_3 Chorismate synthase signature 3. RSDSTavpaAsVVaEAM
ChainResidueDetails
AARG342-MET358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00300
ChainResidueDetails
AARG40
BARG134
BGLN256
BGLY301
BLYS316
BARG342
AARG46
AARG134
AGLN256
AGLY301
ALYS316
AARG342
BARG40
BARG46

237992

PDB entries from 2025-06-25

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