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2BFL

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH5 using 20mM ZnSO4 in buffer. 1mM DTT was used as a reducing agent.

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1296
ChainResidue
AHIS116
AHIS118
AHIS196
AHOH2235
AHOH2236

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1297
ChainResidue
AHOH2238
ACYS221
AHIS263
AHOH2236
AHOH2237

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1298
ChainResidue
ASER225
ATHR226
ASER227
AGLY264
AGLU265
AHOH2239
AHOH2240
AHOH2241

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1299
ChainResidue
ALYS93
AGLU97
AARG131
AILE256
ALYS280
AHOH2060
AHOH2068

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AZI B1295
ChainResidue
BHIS196
BLYS224
BGLY232
BASN233
BZN1299
BHOH2240
BHOH2241

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B1298
ChainResidue
BHIS116
BHIS118
BHIS196
BHOH2241
BHOH2244

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B1299
ChainResidue
BASP120
BCYS221
BHIS263
BAZI1295
BHOH2244
BHOH2245

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B1300
ChainResidue
BSER225
BTHR226
BSER227
BGLY264
BGLU265
BHOH2217
BHOH2246
BHOH2247

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1301
ChainResidue
BLYS181
BLYS186
BARG252
BHOH2248

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1302
ChainResidue
BASN49
BLYS50
BHOH2174

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1292
ChainResidue
ALYS148
BGLU97
BARG107
BARG131

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A1293
ChainResidue
AASN215

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A1294
ChainResidue
ALYS186
AGLN210

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1295
ChainResidue
AALA228
ALYS229
AASP230
AHOH2177
AHOH2234

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1292
ChainResidue
BSER227
BALA228
BLYS229
BASP230
BHOH2236

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B1293
ChainResidue
BASP88
BASP89
BLYS90
BHOH2104

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B1294
ChainResidue
BASN255
BGOL1296
BHOH2238
BHOH2239

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B1296
ChainResidue
BTRP204
BARG252
BTYR253
BARG254
BASN255
BGOL1294
BHOH2242

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B1297
ChainResidue
BLYS129
BGLU168
BGLU169

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1303
ChainResidue
BLYS50
BLYS103
BHOH2031
BHOH2249
BHOH2250

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
AHIS118
AHIS196
BHIS116
BHIS118
BHIS196

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303
ChainResidueDetails
AASP120
ACYS221
AHIS263
BASP120
BCYS221
BHIS263

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

220113

PDB entries from 2024-05-22

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