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1G6S

STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
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 Residues16
DetailsBINDING SITE FOR RESIDUE S3P A 601
ChainResidue
ALYS22
AASP313
AASN336
ALYS340
AGPJ701
AHOH811
AHOH812
AHOH813
ASER23
AARG27
ATHR97
ASER169
ASER170
AGLN171
ASER197
ATYR200

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GPJ A 701
ChainResidue
ALYS22
AASN94
AGLY96
AARG124
AGLN171
AASP313
AGLU341
AARG344
AHIS385
AARG386
ALYS411
AS3P601
AHOH812
AHOH814

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 801
ChainResidue
ATYR335
AHOH986
AHOH1030
AHOH1074
AHOH1365

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 802
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AHOH1208
AHOH1335

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 803
ChainResidue
AASP194
AASN333
AHOH945
AHOH1134
AHOH1177

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 804
ChainResidue
AALA380
ATYR382
AHOH926
AHOH995
AHOH1201

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 805
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH1009
AHOH1137
AHOH1394

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 806
ChainResidue
ALYS38
ATYR335
AHIS363
AHOH1211
AHOH1367

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 807
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH1285

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 808
ChainResidue
AGLU89
ALEU90
APHE91
AHOH890
AHOH1182

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 809
ChainResidue
AGLN145
ATYR237
ALEU238
AHOH1307

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 810
ChainResidue
AALA303
ATHR328
AHOH1045

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 2026-03-25

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