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2BG8

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT and 1mM TCEP-HCl were used as reducing agents.

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 Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1293
ChainResidue
AASP88
AASP89
ALYS90
AHOH2124

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1294
ChainResidue
AHOH2102
ATYR191
AGLY193
ALYS194
AGLU241
AGOL1297

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1295
ChainResidue
ALYS186
AGLN210
AHOH2132

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1296
ChainResidue
AASN75
ALYS106
AHOH2133
AHOH2134
AHOH2135

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1297
ChainResidue
ATYR191
APRO192
AASN248
AGOL1294

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1298
ChainResidue
AHIS116
AHIS118
AHIS196
AHOH2136

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1299
ChainResidue
ASER225
ATHR226
ASER227
AGLY264
AGLU265
AHOH2115
AHOH2137

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1300
ChainResidue
AGLU97
AARG131
AARG254
ALYS280

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1301
ChainResidue
ALYS147
BARG107

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1302
ChainResidue
AHIS196
ACSO221
ALYS224
ALEU231
AGLY232
AASN233
AHIS263
AHOH2136

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1303
ChainResidue
ALYS148
BGLU97
BARG107
BARG131

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1308
ChainResidue
AHOH2143
BGLN47
BLYS103
BPHE104
BHOH2015

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1292
ChainResidue
BALA228
BLYS229
BASP230
BHOH2099

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1293
ChainResidue
BASP88
BASP89
BLYS90
BHOH2142

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1294
ChainResidue
BTHR139
BLEU141
BTYR191

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 1295
ChainResidue
BARG254
BHOH2143

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1296
ChainResidue
BHIS118
BALA119
BTYR167

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 1297
ChainResidue
BHIS116
BHIS118
BHIS196

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1298
ChainResidue
BSER225
BTHR226
BSER227
BGLY264
BGLU265
BHOH2125
BHOH2144

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1299
ChainResidue
BVAL177
BLYS181
BLYS186
BARG252

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1300
ChainResidue
BLYS129
BGLU168
BGLU169

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1301
ChainResidue
BASN49
BLYS50

site_idCC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1302
ChainResidue
BHIS196
BCYS221
BLYS224
BLEU231
BGLY232
BASN233
BHIS263

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
BILE113-GLY133

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK
ChainResidueDetails
APRO209-LYS224
BPRO209-LYS224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:7588620, ECO:0000269|PubMed:9761898
ChainResidueDetails
BHIS116
BHIS118
BHIS196

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303
ChainResidueDetails
BASP120
BCYS221
BHIS263

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
BLYS224

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:9761898
ChainResidueDetails
BASN233

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120
AASN233

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP120
BASN233

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP120

site_idMCSA1
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

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PDB entries from 2024-11-06

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