Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BG6

Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH5 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.

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	HOH2134

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1302

Chain	Residue
A	HOH2041
A	SER225
A	THR226
A	SER227
A	GLY264
A	GLU265

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1303

Chain	Residue
A	LYS93
A	GLU97
A	ARG131
A	ARG254
A	ILE256
A	LYS280
A	HOH2029
A	HOH2033
A	HOH2136

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1304

Chain	Residue
A	THR176
A	HOH2137
A	HOH2138
B	LYS102

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE AZI B 1299

Chain	Residue
B	HIS196
B	CSD221
B	LYS224
B	ASN233
B	HOH2159
B	HOH2160

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE AZI B 1300

Chain	Residue
B	ASN215
B	ASN255

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 1301

Chain	Residue
B	HIS116
B	HIS118
B	HIS196
B	CSD221
B	HOH2162

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1302

Chain	Residue
B	SER225
B	THR226
B	SER227
B	GLY264
B	GLU265
B	HOH2145
B	HOH2163

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1303

Chain	Residue
B	LYS181
B	LYS186
B	ARG252
B	HOH2164

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1304

Chain	Residue
A	LYS148
B	GLU100
B	ARG107
B	ARG131
B	HOH2054

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 1305

Chain	Residue
A	LYS147
B	ARG107

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1306

Chain	Residue
B	LYS129
B	GLU168
B	GLU169

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1293

Chain	Residue
A	ASP88
A	ASP89
A	LYS90

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1294

Chain	Residue
A	LYS186
A	GLN210
A	HOH2130

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1295

Chain	Residue
A	ALA235
A	ALA237
A	TYR238
A	GOL1318
B	LYS291

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1296

Chain	Residue
A	SER227
A	ALA228
A	LYS229
A	ASP230

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1297

Chain	Residue
A	HIS196
A	CSD221
A	LYS224
A	ASN233
B	HOH2073

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1298

Chain	Residue
A	LEU48
A	ASN49
A	GLU130
A	ILE216
A	ASN257
A	ALA258
A	HOH2133

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1299

Chain	Residue
A	HIS118
A	ALA119
A	ASN149
A	TYR167

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1300

Chain	Residue
A	ASN179
A	LEU180
A	LYS181
A	LYS186
B	LYS32
B	VAL34

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1313

Chain	Residue
B	GLN47
B	LYS50
B	LYS103
B	HOH2023

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1318

Chain	Residue
A	GOL1295
A	TYR238

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1293

Chain	Residue
B	ALA228
B	LYS229
B	ASP230
B	HOH2154

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1294

Chain	Residue
B	ALA117
B	HIS118
B	LEU145
B	ASN149
B	THR197
B	ASP199
B	HOH2156

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1295

Chain	Residue
B	ASP88
B	ASP89
B	LYS90
B	HOH2157

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1296

Chain	Residue
B	ASN49
B	LYS50
B	HOH2024

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1297

Chain	Residue
B	GLU100
B	GLN105
B	ARG107
B	HOH2055

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1298

Chain	Residue
B	VAL54
B	ASN70
B	GLY264
B	GLU265
B	HOH2158

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 site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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	ALA237	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	ALA237	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)