Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AAY

EPSP synthase liganded with shikimate and glyphosate

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 Residues12
DetailsBINDING SITE FOR RESIDUE SKM A 701
ChainResidue
ALYS22
AFMT902
AFMT904
AHOH915
ASER23
AARG27
ATHR97
AGLN171
ATYR200
AASP313
ALYS340
AGPJ702

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GPJ A 702
ChainResidue
ALYS22
AASN94
AGLY96
AARG124
AGLN171
AASP313
AGLU341
AARG344
AHIS385
AARG386
ALYS411
ASKM701
AHOH920
AHOH1200

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 901
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH1063
AHOH1148
AHOH1207

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 902
ChainResidue
AARG100
ASER169
AGLN171
ALYS340
ASKM701
AHOH969
AHOH1200

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 903
ChainResidue
ATHR5
ATHR141
ALEU143
AARG152
APHE376
ATHR402

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 904
ChainResidue
AVAL168
ASER170
ASER197
AASN336
ALYS340
ASKM701

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 905
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH1150
AHOH1368

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 906
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AHOH1214
AHOH1279

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 907
ChainResidue
AGLU300
ALEU301
ALYS326
AHOH1236
AHOH1296

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 908
ChainResidue
AALA380
ATYR382
AHOH985
AHOH1181
AHOH1338

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 909
ChainResidue
AGLU89
ALEU90
APHE91
AHOH964
AHOH1421

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
AASP313

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
AASP313
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
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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon