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2O0X

Mycobacterium tuberculosis epsp synthase in complex with intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
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 Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG68
AHOH749
AHOH935
AGLY142
ATHR143
AGLY144
AHOH542
AHOH572
AHOH652
AHOH655
AHOH732

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG278
AHIS286
AARG354
AARG379
AHOH540
AHOH644
AHOH841
AHOH953
AHOH1103

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE SKP A 501
ChainResidue
ALYS23
ASER24
AARG28
ALEU94
AGLY96
ATHR97
APHE101
AARG124
ASER167
ASER168
AGLN169
ASER196
AHIS199
AGLU311
AHIS336
AHIS340
AGLU341
AARG344
AHIS384
AARG385
ALYS410
AHOH508
AHOH530
AHOH584
AHOH596
AHOH614
AHOH683

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. VDcGLAGTVLRfVpP
ChainResidueDetails
AVAL90-PRO104

site_idPS00885
Number of Residues19
DetailsEPSP_SYNTHASE_2 EPSP synthase signature 2. RgHETDRLaALsteInrLG
ChainResidueDetails
AARG338-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Complex of 3-phosphoshikimate 1-carboxyvinyltransferase.","authors":["Kachalova G.S.","Burenkov G.P.","Strizhov N.I.","Brunning M.G.","Bartunik H.D."]}},{"source":"PDB","id":"2O0E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Complex of 3-phosphoshikimate 1-carboxyvinyltransferase.","authors":["Kachalova G.S.","Burenkov G.P.","Strizhov N.I.","Brunning M.G.","Bartunik H.D."]}},{"source":"PDB","id":"2O0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O0E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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