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2X71

Structural basis for the interaction of lactivicins with serine beta- lactamases

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE L4C A 1291
ChainResidue
ASER70
AGLY236
AALA237
AARG244
AHOH2091
AHOH2135
AASN104
ATYR105
ASER130
AASN132
AASN170
ATHR216
ALYS234
ATHR235

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1291
ChainResidue
BSER70
BSER130
BLYS234
BTHR235
BGLY236
BALA237
BARG244
BHOH2034

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EOH A 1292
ChainResidue
ALYS140
AGLY143
AGLY144
APHE165
BGLY143
BGLY144
BPHE165

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH A 1293
ChainResidue
ALYS288
AALA289
AHOH2167

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH B 1292
ChainResidue
BLYS288
BLEU290

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH B 1293
ChainResidue
BLYS273
BTYR274
BHOH2137

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVT
ChainResidueDetails
APHE47-THR59

site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL
ChainResidueDetails
APHE66-LEU81

219140

PDB entries from 2024-05-01

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