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2QFS

E.coli EPSP synthase Pro101Ser liganded with S3P

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE S3P A 701
ChainResidue
ALYS22
AASP313
AASN336
ALYS340
AFMT601
AHOH729
AHOH730
AHOH740
AHOH963
ASER23
AARG27
ATHR97
ASER169
ASER170
AGLN171
ASER197
ATYR200

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 601
ChainResidue
ALYS22
AASP313
AGLU341
AARG344
AHIS385
AARG386
AS3P701

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 602
ChainResidue
ALYS22
AASN94
AGLY96
ATHR97
AARG124
AGLN171
AGLU341
ALYS411
AHOH705

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 603
ChainResidue
AALA380
ATYR382
AHOH779
AHOH915
AHOH1023

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 604
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH880
AHOH1101
AHOH1110

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 605
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH1128
AHOH1154

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 606
ChainResidue
ATHR5
ATHR141
ALEU143
AARG152
APHE376
ATHR402
AHOH1015
AHOH1066
AHOH1210

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 607
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AGLU74
AHOH939
AHOH1286

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 608
ChainResidue
AARG11
AASP13
ATYR220
AGLN425
AHOH1196
AHOH1222

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 609
ChainResidue
ALYS38
ATYR335
AHIS363
AHOH1086
AHOH1172
AHOH1245
AHOH1259

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 610
ChainResidue
AARG298
AGLU300
ALEU301
APHE324
AHOH991
AHOH1279

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 611
ChainResidue
AASP13
AGLY14
ATHR259
AHOH1185

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FMT A 612
ChainResidue
AHOH1198
AHIS36
AGLY79
AGLY80
ALEU182
ASER230
AHOH737
AHOH888
AHOH891
AHOH1022

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGTAMRsLaA
ChainResidueDetails
ALEU90-ALA104

site_idPS00885
Number of Residues19
DetailsEPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRLfAMateLrkVG
ChainResidueDetails
AARG338-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"13129913","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11171958","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G6S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Modified by bromopyruvate","evidences":[{"source":"PubMed","id":"11171958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g6t
ChainResidueDetails
ALYS22
AASP313
ALYS411
AHIS385
AGLU341

site_idMCSA1
Number of Residues7
DetailsM-CSA 457
ChainResidueDetails
AASP49metal ligand
AASN94metal ligand
AASP313electrostatic stabiliser, proton shuttle (general acid/base)
AGLU341electrostatic stabiliser, metal ligand, proton shuttle (general acid/base)
AHIS385steric role
AARG386transition state stabiliser
ALYS411steric role

238895

PDB entries from 2025-07-16

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