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1Q36

EPSP synthase (Asp313Ala) liganded with 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
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE SKP A 600
ChainResidue
ALYS22
AGLN171
ASER197
ATYR200
AASN336
ALYS340
AGLU341
AARG344
AHIS385
AARG386
ALYS411
ASER23
AHOH621
AHOH629
AHOH641
AHOH681
AHOH712
AARG27
AASN94
AGLY96
ATHR97
AARG124
ASER169
ASER170

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 601
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH740
AHOH907
AHOH915

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 602
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH904
AHOH1058

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 603
ChainResidue
ATHR5
ALEU143
AARG152
APHE376
ATHR402

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 604
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AHOH980
AHOH1046

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 605
ChainResidue
ALEU60
AHIS83
AHOH781
AHOH813
AHOH986
AHOH1147

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 606
ChainResidue
AGLY264
AILE265
AGLY266
ASER269
AHOH747
AHOH888
AHOH1022
AHOH1028

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 607
ChainResidue
ALEU88
AHOH709
AHOH787
AHOH813
AHOH889

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 608
ChainResidue
ALEU135
AGLY137
AHOH824
AHOH847
AHOH1138

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 609
ChainResidue
AALA380
ATYR382
AHOH701
AHOH792
AHOH994

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
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:13129913
ChainResidueDetails
AALA313

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210
ChainResidueDetails
ALYS22
AGLY96
AARG124
AGLN171
AARG344
AARG386
ALYS411

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
ChainResidueDetails
ASER23
AARG27
ASER169
ASER170
ASER197
AALA313
AASN336
ALYS340

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Modified by bromopyruvate => ECO:0000269|PubMed:11171958
ChainResidueDetails
ACYS408
ALYS411

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g6t
ChainResidueDetails
ALYS22
AALA313
ALYS411
AHIS385
AGLU341

site_idMCSA1
Number of Residues7
DetailsM-CSA 457
ChainResidueDetails
AASP49metal ligand
AASN94metal ligand
AALA313electrostatic 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 2024-07-10

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