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1X8R

EPSPS liganded with the (S)-phosphonate analog of the tetrahedral reaction intermediate

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 Residues24
DetailsBINDING SITE FOR RESIDUE SC1 A 601
ChainResidue
ALYS22
AGLN171
ASER197
ATYR200
AASP313
AASN336
ALYS340
AGLU341
AARG344
AHIS385
AARG386
ASER23
ALYS411
AHOH716
AHOH719
AHOH785
AHOH860
AARG27
AASN94
AGLY96
ATHR97
AARG124
ASER169
ASER170

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 701
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH849
AHOH973

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 702
ChainResidue
ATYR382
AHOH793
AHOH1018
AHOH1048

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 703
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH1059
AHOH1232

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 704
ChainResidue
ATHR5
ATHR141
ALEU143
AARG152
APHE376
ATHR402
AHOH1029
AHOH1149
AHOH1254

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 705
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AGLU74
AHOH1103

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 706
ChainResidue
AGLU358
AGLU360
AARG367
ATHR369
AHOH873

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 707
ChainResidue
AARG298
ALEU301
APHE324
AHOH949
AHOH1052

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 708
ChainResidue
AGLU240
AGLY264
AILE265
AGLY266
ASER269
AHOH865
AHOH909
AHOH1004
AHOH1157

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 709
ChainResidue
ALEU18
APRO19
AASN43
ATHR71
AHOH829
AHOH1199
AHOH1209

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 710
ChainResidue
ALYS38
ATYR335
AHIS363
AHOH1150
AHOH1190

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 711
ChainResidue
AHOH856
AHOH912
AHOH1076

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 712
ChainResidue
AARG332
ATYR365
AARG367
AHOH1279

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGTAMRpLaA
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

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PDB entries from 2026-01-21

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