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5BUF

2.37 Angstrom Structure of EPSP Synthase from acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0009073biological_processaromatic amino acid family biosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0003824molecular_functioncatalytic activity
B0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
B0009073biological_processaromatic amino acid family biosynthetic process
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CL A 801
ChainResidue
AARG339
AARG508
AHIS510
ATHR511
AHOH1061
AHOH1122

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 802
ChainResidue
AARG661
AARG710

site_idAC3
Number of Residues4
Detailsbinding site for residue CL B 801
ChainResidue
BHIS510
BTHR511
BHOH1059
BARG339

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 802
ChainResidue
BGLU658
BARG661
BHIS709
BARG710

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LYmGNSGTSMRlLsG
ChainResidueDetails
ALEU401-GLY415

site_idPS00885
Number of Residues19
DetailsEPSP_SYNTHASE_2 EPSP synthase signature 2. RvKESDRIqVMadgLkiMG
ChainResidueDetails
AARG655-GLY673

237992

PDB entries from 2025-06-25

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