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6PT5

Crystal Structure of Class D Beta-lactamase OXA-48 with Cefoxitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
AARG206
CARG206

site_idAC2
Number of Residues11
Detailsbinding site for residue 1S7 A 302
ChainResidue
ATYR211
ATHR213
AARG214
AARG250
ASER70
ATRP105
ASER118
AVAL120
ALEU158
ATHR209
AGLY210

site_idAC3
Number of Residues2
Detailsbinding site for residue CL B 301
ChainResidue
BARG206
DARG206

site_idAC4
Number of Residues15
Detailsbinding site for Di-peptide 1S7 B 302 and SER B 70
ChainResidue
BPRO68
BALA69
BTHR71
BPHE72
BLYS73
BSER118
BVAL120
BLEU158
BLYS208
BTHR209
BGLY210
BTYR211
BTHR213
BARG214
BARG250

site_idAC5
Number of Residues18
Detailsbinding site for Di-peptide 1S7 B 302 and ARG B 250
ChainResidue
BALA69
BSER70
BSER118
BVAL120
BLEU158
BTHR209
BGLY210
BTYR211
BTHR213
BARG214
BTRP221
BMET237
BLEU247
BGLY248
BLEU249
BGLN251
BALA252
BTHR254

site_idAC6
Number of Residues18
Detailsbinding site for Di-peptide 1S7 C 301 and ARG C 250
ChainResidue
CALA69
CSER70
CSER118
CVAL120
CLEU158
CTHR209
CGLY210
CTYR211
CSER212
CTHR213
CARG214
CTRP221
CLEU247
CGLY248
CLEU249
CGLN251
CALA252
CTHR254

site_idAC7
Number of Residues16
Detailsbinding site for Di-peptide 1S7 C 301 and SER C 70
ChainResidue
CPRO68
CALA69
CTHR71
CPHE72
CLYS73
CSER118
CVAL120
CLEU158
CLYS208
CTHR209
CGLY210
CTYR211
CSER212
CTHR213
CARG214
CARG250

site_idAC8
Number of Residues15
Detailsbinding site for Di-peptide 1S7 D 301 and SER D 70
ChainResidue
DPRO68
DALA69
DTHR71
DPHE72
DLYS73
DSER118
DVAL120
DLEU158
DLYS208
DTHR209
DGLY210
DTYR211
DTHR213
DARG214
DARG250

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL
ChainResidueDetails
APRO68-LEU78

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PDB entries from 2024-10-02

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