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2BG7

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1293
ChainResidue
AASN215
AHOH2147

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1294
ChainResidue
AHIS196
ACSO221
ALYS224
AASN233
AHIS263
AHOH2116

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1295
ChainResidue
BGLU97
BARG107
BARG131
ALYS148

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1296
ChainResidue
ALYS186
AGLN210
AHOH2164

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1297
ChainResidue
AALA235
AASP236
AALA237
ATYR238
AHOH2165
BLYS291

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1298
ChainResidue
AHIS118
AALA119
ATYR167

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1299
ChainResidue
AHIS116
AHIS118
AHIS196
AHOH2166

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1300
ChainResidue
ASER225
ATHR226
ASER227
AGLY264
AGLU265
AHOH2155
AHOH2167
AHOH2168
AHOH2169

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1301
ChainResidue
ALYS93
AGLU97
AARG131
AILE256
ALYS280
AHOH2045
AHOH2049
AHOH2170

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1293
ChainResidue
BALA228
BLYS229
BASP230
BHOH2162

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1294
ChainResidue
BLYS129
BLYS147
BGLU168
BGLU169

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 1295
ChainResidue
BASN215
BASN255

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1296
ChainResidue
BHIS196
BCSO221
BGLY232
BASN233
BHOH2128
BHOH2174

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1297
ChainResidue
BASP88
BASP89
BLYS90

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1298
ChainResidue
BLYS78
BTHR176
BGLY183

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1299
ChainResidue
BHIS116
BHIS118
BHIS196
BHOH2174

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1300
ChainResidue
BLYS181
BLYS186
BARG252

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1301
ChainResidue
BSER225
BTHR226
BSER227
BGLY264
BGLU265
BHOH2165
BHOH2177
BHOH2178

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADciGGiktlker.G
ChainResidueDetails
AILE113-GLY133

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK
ChainResidueDetails
APRO209-LYS224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:7588620, ECO:0000269|PubMed:9761898
ChainResidueDetails
AHIS116
BHIS118
BHIS196
AHIS118
AHIS196
BHIS116

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303
ChainResidueDetails
AHIS263
BASP120
BCSO221
BHIS263
AASP120
ACSO221

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
ALYS224
BLYS224

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:9761898
ChainResidueDetails
AASN233
BASN233

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS196metal ligand
AASN233electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
BHIS116metal ligand
BHIS118metal ligand
BASP120hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS196metal ligand
BASN233electrostatic stabiliser, hydrogen bond donor

219869

PDB entries from 2024-05-15

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