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

2O15

Mycobacterium tuberculosis epsp synthase after partial products withdrawal

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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG278
AHIS286
AARG379

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AGLN169
ALYS410
ALYS23
AASP54
ALEU94
AALA95
AGLY96
ATHR97

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
ASER24
AARG28
ATHR97
AGLN169
AHIS199
AHOH662

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

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon