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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BG2

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20mM ZnSO4 in the buffer. 1mM DTT and 1mM TCEP- HCl were used as reducing agents. Cys221 is reduced.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0008270	molecular_function	zinc ion binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1301

Chain	Residue
A	HIS116
A	HIS118
A	HIS196
A	GOL1296

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1302

Chain	Residue
A	CYS221
A	HIS263
A	GOL1296
A	HOH2156

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1303

Chain	Residue
A	THR226
A	SER227
A	GLU265
A	HOH2139
A	SER225

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1304

Chain	Residue
A	LYS93
A	GLU97
A	ARG131
A	ARG254
A	ILE256
A	LYS280
A	HOH2037
A	HOH2157
A	HOH2158

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1301

Chain	Residue
B	CYS221
B	HIS263
B	CL1303
B	HOH2141

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1302

Chain	Residue
B	HIS116
B	HIS118
B	HIS196
B	CL1303

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1304

Chain	Residue
B	SER225
B	THR226
B	SER227
B	GLY264
B	GLU265
B	HOH2142

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 1305

Chain	Residue
A	LYS147
B	ARG107

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1306

Chain	Residue
B	ASN49
B	LYS50
B	TYR211
B	HOH2143

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1307

Chain	Residue
A	GOL1298
B	SER227
B	ALA228
B	LYS229
B	ASP230

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1308

Chain	Residue
B	LYS181
B	LYS186
B	ARG252

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 1303

Chain	Residue
B	ASP120
B	ZN1301
B	ZN1302

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1292

Chain	Residue
A	ALA117
A	LEU145
A	ASN149
A	THR197
A	ASP199
A	ASP236
A	HOH2146

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1293

Chain	Residue
A	LYS148
B	GLU97
B	ARG107
B	ARG131

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1294

Chain	Residue
A	ASP88
A	ASP89
A	LYS90

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1295

Chain	Residue
A	TRP204
A	PRO209
A	ASN215
A	GOL1297
A	HOH2101
A	HOH2147

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1296

Chain	Residue
A	TRP87
A	HIS118
A	ASP120
A	CYS221
A	ZN1301
A	ZN1302
A	HOH2152

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1297

Chain	Residue
A	ASN215
A	GOL1295
A	HOH2154

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1298

Chain	Residue
A	ASN233
A	HOH2152
B	ASP230
B	SO41307

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1299

Chain	Residue
A	ASP111
A	LYS181
A	PHE182
B	LYS32

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1300

Chain	Residue
A	ALA235
A	ALA237
B	ASP288

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1319

Chain	Residue
A	TYR238
A	HOH2159

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1292

Chain	Residue
B	ASP88
B	ASP89
B	LYS90

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1293

Chain	Residue
B	LYS129
B	GLU168
B	GLU169

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1294

Chain	Residue
B	TYR191
B	PRO192
B	ASN248

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1295

Chain	Residue
B	ARG254
B	ASN255
B	LYS280

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1296

Chain	Residue
B	THR139
B	LEU141
B	HOH2134

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1297

Chain	Residue
B	HIS118
B	ALA119
B	TYR167
B	HOH2138

site_id	DC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1298

Chain	Residue
B	ASN215
B	ARG254
B	ASN255

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1299

Chain	Residue
B	VAL54
B	GLU265
B	HOH2140

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1300

Chain	Residue
B	GLU100
B	GLN105
B	LYS106
B	ARG107

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1309

Chain	Residue
A	HOH2082
B	GLN47
B	TRP53
B	LYS103
B	PHE104
B	HOH2020

site_id	DC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 1320

Chain	Residue
B	LYS148

Functional Information from PROSITE/UniProt

site_id	PS00743
Number of Residues	20
Details	BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADciGGiktlker.G

Chain	Residue	Details
A	ILE113-GLY133

site_id	PS00744
Number of Residues	13
Details	BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK

Chain	Residue	Details
A	PRO209-LYS224

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:20677753, ECO:0000269\|PubMed:24059435, ECO:0000269\|PubMed:26482303, ECO:0000269\|PubMed:7588620, ECO:0000269\|PubMed:9761898

Chain	Residue	Details
A	HIS116
A	HIS118
A	HIS196
B	HIS116
B	HIS118
B	HIS196

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:20677753, ECO:0000269\|PubMed:24059435, ECO:0000269\|PubMed:26482303

Chain	Residue	Details
A	ASP120
A	CYS221
A	HIS263
B	ASP120
B	CYS221
B	HIS263

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:26482303

Chain	Residue	Details
A	LYS224
B	LYS224

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:26482303, ECO:0000269\|PubMed:9761898

Chain	Residue	Details
A	ASN233
B	ASN233

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
A	ASP120
A	ASN233

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
B	ASP120
B	ASN233

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
A	ASP120

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
B	ASP120

site_id	MCSA1
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
A	HIS116	metal ligand
A	HIS118	metal ligand
A	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS196	metal ligand
A	ASN233	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
B	HIS116	metal ligand
B	HIS118	metal ligand
B	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS196	metal ligand
B	ASN233	electrostatic stabiliser, hydrogen bond donor

222926

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