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3FJZ

E. coli EPSP synthase (T97I) liganded with S3P and glyphosate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003855molecular_function3-dehydroquinate dehydratase activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0004764molecular_functionshikimate 3-dehydrogenase (NADP+) activity
A0004765molecular_functionshikimate kinase 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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GPF A 429
ChainResidue
ALYS22
AARG386
ALYS411
AS3P430
AHOH563
AHOH599
AASN94
AGLY96
AARG124
AGLN171
AASP313
AGLU341
AARG344
AHIS385

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE S3P A 430
ChainResidue
ALYS22
ASER23
AARG27
AILE97
ASER169
ASER170
AGLN171
ASER197
ATYR200
AASP313
AASN336
ALYS340
AGPF429
AHOH519
AHOH522
AHOH599

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 431
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AHOH873

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 432
ChainResidue
ATHR5
ATHR141
ALEU143
AARG152
ATHR402
AHOH758

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 433
ChainResidue
AGLU300
ALEU301
APHE324
AHOH474
AHOH824

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 434
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH923

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 435
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH731
AHOH820
AHOH849

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 436
ChainResidue
ALYS38
ATYR335
AHIS363

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 437
ChainResidue
ALYS38
ATYR335
AHOH669
AHOH789

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 438
ChainResidue
AGLN145
ATYR237
ALEU238
AHOH464
AHOH847

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGIAMRpLaA
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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556
ChainResidueDetails
AASP313

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:15736934, ECO:0000305|PubMed:11171958
ChainResidueDetails
AGLU341

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556
ChainResidueDetails
ALYS22
ASER169
ALYS340

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556
ChainResidueDetails
AARG27
ASER197
AASN336

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556
ChainResidueDetails
AARG124
AARG344
AARG386
ALYS411

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Modified by bromopyruvate => ECO:0000269|PubMed:11171958
ChainResidueDetails
ACYS408
ALYS411

Catalytic Information from CSA
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

217705

PDB entries from 2024-03-27

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