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3FK0

E. coli EPSP synthase (TIPS mutation) 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 428
ChainResidue
ALYS22
AASP313
AASN336
ALYS340
AFMT430
AHOH551
AHOH553
AHOH825
AHOH839
ASER23
AARG27
AILE97
ASER169
ASER170
AGLN171
ASER197
ATYR200

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 429
ChainResidue
AALA380
ATYR382
AHOH467
AHOH558
AHOH807

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 430
ChainResidue
ALYS22
AASP313
AGLU341
AARG344
AHIS385
AARG386
AS3P428

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 431
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH685
AHOH843

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 432
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AFMT436

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 433
ChainResidue
AARG298
AGLU300
ALEU301
APHE324
AHOH918

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 434
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH850

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 435
ChainResidue
ATHR5
ALEU143
AARG152
APHE376
ATHR402

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 436
ChainResidue
AFMT432
AHOH513
AHOH701

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 437
ChainResidue
ALYS38
AHIS363
AHOH937

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGIAMRsLaA
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 2025-10-08

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