Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AA9

EPSP synthase liganded with shikimate

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 Residues14
DetailsBINDING SITE FOR RESIDUE SKM A 501
ChainResidue
ALYS22
AFMT602
AFMT603
AFMT611
AHOH638
AHOH678
ASER23
AARG27
ATHR97
AGLN171
ATYR200
AASP313
ALYS340
AFMT601

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 601
ChainResidue
ALYS22
AASP313
AGLU341
AARG344
AHIS385
AARG386
ASKM501

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 602
ChainResidue
AARG100
ASER169
AGLN171
ALYS340
ASKM501
AHOH672
AHOH681

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 603
ChainResidue
ASER170
ASER197
AASN336
ALYS340
ASKM501

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 604
ChainResidue
AALA380
ATYR382
AHOH698
AHOH843
AHOH933

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FMT A 605
ChainResidue
ATHR5
ALEU143
AARG152
AARG267
AASN268
APHE376
ATHR402
APHE417
AGLU418
AALA421
AHOH661
AHOH708
AHOH897
AHOH997

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 606
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH767
AHOH949
AHOH1057

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 607
ChainResidue
AGLU341
ATHR342
ATYR382
AHOH780
AHOH924

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 608
ChainResidue
ALEU60
AHIS83
AHOH752
AHOH802
AHOH1077

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 609
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AGLU74
AHOH948

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 610
ChainResidue
ALYS38
ATYR335
AHIS363
AHOH965
AHOH1102

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 611
ChainResidue
ALYS22
AASN94
AGLY96
AARG124
AGLU341
ALYS411
ASKM501
AHOH619

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 612
ChainResidue
APRO81
AHIS83
AGLY109
AHOH986

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 613
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64
AHOH957

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 614
ChainResidue
AHOH766
AHOH805
AASN161
AGLU358

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 615
ChainResidue
AASN78
AHOH1023

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 616
ChainResidue
AASN43
ALEU238
AVAL239
AGLU240
AGLY241
AGLY264
AASP292
AHOH886
AHOH1104

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 617
ChainResidue
AASN55
AGLU89
ALEU90
APHE91
AHOH699
AHOH1000

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

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon