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2O0E

Mycobacterium tuberculosis epsp synthase in complex with S3P and PEP

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG68
AGLY142
ATHR143
AGLY144
AHOH575
AHOH655
AHOH658
AHOH752

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AHIS286
AARG379
AHOH543
AHOH647
AHOH704
AHOH784
AHOH825
AHOH844
AHOH928
AHOH956
AARG278

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ALYS23
ALEU94
AALA95
AGLY96
ATHR97
AARG124
AGLN169
AGLU341
ALYS410
AHOH599
AHOH1112

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE S3P A 501
ChainResidue
ALYS23
ASER24
AARG28
ATHR97
APHE101
ASER167
ASER168
AGLN169
ASER196
AHIS199
AGLU311
AHIS336
AHIS340
AHOH506
AHOH512
AHOH587
AHOH599
AHOH617

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PEP A 502
ChainResidue
ALYS23
ALEU94
AGLY96
AARG124
AGLN169
AGLU311
AGLU341
AARG344
AHIS384
AARG385
ALYS410
AHOH599
AHOH1111
AHOH1112

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

247536

PDB entries from 2026-01-14

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