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2WK0

Crystal structure of the class A beta-lactamase BS3 inhibited by 6- beta-iodopenicillanate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0005886cellular_componentplasma membrane
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 Residues12
DetailsBINDING SITE FOR RESIDUE BIY A 300
ChainResidue
AALA69
ACL301
AHOH2116
AHOH2201
ASER70
AASN104
ATYR105
ASER130
AASN132
AASN170
AGLY236
AALA237

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
ABIY300

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BIY B 300
ChainResidue
BALA69
BSER70
BASN104
BTYR105
BSER130
BASN132
BASN170
BGLY236
BALA237
BCL301
BHOH2076
BHOH2156
BHOH2157

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 301
ChainResidue
BSER70
BSER130
BLYS234
BTHR235
BBIY300

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT B 1292
ChainResidue
AASN161
AGLU163
AGLU176
ATHR177
AGLN178
AHOH2120
BGLU171
BASN173
BHOH2158

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1292
ChainResidue
ALYS140
AGLY143
AGLY144
APHE165
AHOH2202
AHOH2203
BLYS140
BPHE165

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH A 1293
ChainResidue
AALA42
AARG61

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH A 1294
ChainResidue
AASP32
ALYS35
AHOH2204

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH A 1295
ChainResidue
AASN173
AGLU176

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EOH B 1293
ChainResidue
BARG65
BVAL172
BHOH2035
BHOH2084
BHOH2120
BHOH2160

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70
BSER70

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU168
BGLU168

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS234
BLYS234

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AGLU166
ALYS73
ASER130
ASER70

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BGLU166
BLYS73
BSER130
BSER70

222036

PDB entries from 2024-07-03

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