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1UM0

Crystal structure of chorismate synthase complexed with FMN

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
C0004107molecular_functionchorismate synthase activity
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0010181molecular_functionFMN binding
C0016829molecular_functionlyase activity
D0004107molecular_functionchorismate synthase activity
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0009423biological_processchorismate biosynthetic process
D0010181molecular_functionFMN binding
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 1400
ChainResidue
ASER103
APRO299
ASER300
AILE327
AARG330
AHOH1420
AHOH1432
AHOH1436
AHOH1529
DLEU280
DGLY281
AHIS104
AARG123
ASER125
ALEU240
AASN241
AGLY242
ALYS296
ATHR298

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN B 2400
ChainResidue
BSER103
BHIS104
BARG123
BSER125
BLEU240
BASN241
BLYS296
BTHR298
BPRO299
BSER300
BILE327
BARG330
BHOH2411
BHOH2434
BHOH2458
BHOH2460
BHOH2481
CLEU280
CGLY281
CGLY282

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN C 3400
ChainResidue
BLEU280
BGLY281
CARG50
CSER103
CHIS104
CARG123
CSER125
CLEU240
CASN241
CGLY242
CLYS296
CTHR298
CPRO299
CSER300
CILE327
CHOH3419

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN D 4400
ChainResidue
ALEU280
AGLY281
DSER103
DHIS104
DARG123
DSER125
DLEU240
DASN241
DGLY242
DLYS296
DTHR298
DPRO299
DSER300
DILE327
DARG330
DHOH4414
DHOH4433
DHOH4476
DHOH4514

Functional Information from PROSITE/UniProt
site_idPS00787
Number of Residues16
DetailsCHORISMATE_SYNTHASE_1 Chorismate synthase signature 1. GESHGdvIGgVLDGmP
ChainResidueDetails
AGLY14-PRO29

site_idPS00788
Number of Residues17
DetailsCHORISMATE_SYNTHASE_2 Chorismate synthase signature 2. GrsSAReSairVaaGAF
ChainResidueDetails
AGLY122-PHE138

site_idPS00789
Number of Residues17
DetailsCHORISMATE_SYNTHASE_3 Chorismate synthase signature 3. RHDPCiairGsVVcESL
ChainResidueDetails
AARG322-LEU338

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00300","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00300","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15095868","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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