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2NZE

Structure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group P3121.

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 A 401
ChainResidue
AHIS86
AHIS88
AHIS149
AHOH726
AHOH812

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BHOH816
BHIS86
BHIS88
BHIS149
BHOH785

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ASER172
ATHR173
ASER174
AGLY211
AGLU212
AHOH773
AHOH845

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BSER172
BTHR173
BSER174
BGLY211
BGLU212
BHOH706

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ALYS65
AGLU69
AARG101
AILE203
ALYS216
AHOH744
AHOH806

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BLYS134
BLYS139
BARG199

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ASER168
ALYS171
AHIS210
AHOH750
AHOH765

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 506
ChainResidue
BSER168
BLYS171
BGLY209
BHIS210
BHOH732
BHOH743
BHOH850

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 601
ChainResidue
BASP60
BASP61
BLYS62

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 602
ChainResidue
ALYS99
AGLU121

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 603
ChainResidue
AASN162

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 604
ChainResidue
BLYS99
BGLU121
BGLU122

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY B 605
ChainResidue
BASN162
BASN202

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 606
ChainResidue
BALA175
BLYS176
BASP177
BHOH854

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 607
ChainResidue
AASP60
AASP61
ALYS62

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 608
ChainResidue
AALA175
ALYS176
AASP177
AHOH873

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AASN137
ALYS139
AGLN160
AHOH740

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
AALA182
AASP183
AALA184
ATYR185
AHOH832
AHOH874
BLYS227

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 703
ChainResidue
BTHR29
BASN42
BGLY211
BGLU212
BVAL213
BHOH720
BHOH723
BHOH894

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADhiGGiktlker.G
ChainResidueDetails
AILE83-GLY102

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
AHIS86
AHIS88
AHIS149
BHIS86
BHIS88
BHIS149

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303
ChainResidueDetails
AASP90
ASER168
AHIS210
BASP90
BSER168
BHIS210

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
ALYS171
BLYS171

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:9761898
ChainResidueDetails
AASN180
BASN180

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP90
AASN180

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP90
BASN180

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP90

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP90

site_idMCSA1
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
AHIS86metal ligand
AHIS88metal ligand
AASP90hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS149metal ligand
AASN180electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
BHIS86metal ligand
BHIS88metal ligand
BASP90hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS149metal ligand
BASN180electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-06-11

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