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

1MI4

Glyphosate insensitive G96A mutant EPSP synthase liganded with shikimate-3-phosphate

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 1001
ChainResidue
ALYS22
AASP313
AASN336
ALYS340
AFMT2001
AHOH2029
AHOH2030
AHOH2058
AHOH2071
ASER23
AARG27
ATHR97
ASER169
ASER170
AGLN171
ASER197
ATYR200

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT A 2001
ChainResidue
ALYS22
AASP313
AGLU341
AARG344
AHIS385
AARG386
AS3P1001

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 2002
ChainResidue
ALYS22
AASN94
AALA96
ATHR97
AARG124
AGLU341
ALYS411
AHOH2016

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2003
ChainResidue
AALA380
ATYR382
AHOH2063
AHOH2329
AHOH2390

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2004
ChainResidue
ALYS373
ALEU374
ASER397
AASP398
AHOH2145

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2005
ChainResidue
ATHR65
ALEU66
ASER67
AARG72
AHOH2325

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 2006
ChainResidue
ATYR335
AHOH2255
AHOH2271

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2007
ChainResidue
AGLU89
ALEU90
APHE91
AHOH2124

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2008
ChainResidue
ATHR58
AVAL62
ASER63
ATYR64

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 2009
ChainResidue
AGLU300
ALEU301
APHE324
AHOH2316
AHOH2389

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 2010
ChainResidue
AASP13
AGLY14
ATHR259

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 2011
ChainResidue
ATHR5
ALEU143
AARG152
APHE376
ATHR402
AHOH2308

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 2012
ChainResidue
AALA303
ATHR328
AHOH2253

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2013
ChainResidue
AGLN145
ATYR237
ALEU238
AHOH2365

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 2014
ChainResidue
APRO8
AILE9
AALA10
AGLN425
AALA426
AHOH2121
AHOH2384
AHOH2433

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAATAMRpLaA
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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon