Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KNS

Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)

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
C	0008270	molecular_function	zinc ion binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0042597	cellular_component	periplasmic space
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
D	0008270	molecular_function	zinc ion binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0042597	cellular_component	periplasmic space
D	0046677	biological_process	response to antibiotic
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 228

Chain	Residue
A	HIS86
A	HIS88
A	HIS149
A	HOH267
A	HOH737

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 229

Chain	Residue
A	HOH267
A	ASP90
A	ASP168
A	HIS210
A	ACY233

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 230

Chain	Residue
A	THR131
A	ASN132
A	HOH333
A	HOH788
A	HOH1317
C	HOH310
C	HOH629

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 231

Chain	Residue
A	LYS198
A	HOH1254
A	HOH1267
C	ASN162
C	ASN202
C	HOH268
C	HOH464
C	HOH481

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 232

Chain	Residue
A	HOH297
A	HOH777
A	HOH1284
C	THR131
C	ASN132
C	HOH288
C	HOH308

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY A 233

Chain	Residue
A	ASP90
A	ASP168
A	HIS210
A	ZN229
A	HOH267
A	HOH671
A	HOH737
A	HOH1139

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 234

Chain	Residue
A	ASP60
A	ASP61
A	LYS62
A	HOH454
A	HOH757
A	HOH1001
A	HOH1003

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 235

Chain	Residue
A	ASN162
A	ASN202
A	HOH1029
A	HOH1226
A	HOH1274
C	LYS198

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 236

Chain	Residue
A	ARG199
A	TYR200
A	HOH273
A	HOH334
A	HOH1259
C	ASN195
C	LYS198
C	HOH242
C	HOH645

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 237

Chain	Residue
A	ASN195
A	LYS198
A	HOH269
A	HOH620
A	HOH1242
C	ARG199
C	TYR200
C	HOH290
C	HOH306
C	HOH464

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 228

Chain	Residue
B	HIS86
B	HIS88
B	HIS149
B	ASP168
B	HOH279
B	HOH743

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 229

Chain	Residue
B	ASP90
B	ASP168
B	HIS210
B	HOH743
B	HOH744

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 230

Chain	Residue
B	ASN162
B	ASN202
B	HOH239
B	HOH887

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY B 231

Chain	Residue
B	LYS139
B	GLN160
B	HOH1175
B	HOH1404
B	HOH1408

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY B 232

Chain	Residue
B	SER172
B	THR173
B	SER174
B	GLU212
B	HOH257
C	GLY36

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 228

Chain	Residue
C	HIS88
C	HIS149
C	HOH519
C	HOH915
C	HIS86

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 229

Chain	Residue
C	ASP90
C	ASP168
C	HIS210
C	ACY230
C	HOH519

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY C 230

Chain	Residue
C	ASP90
C	ASP168
C	HIS210
C	ZN229
C	HOH276
C	HOH519
C	HOH915
C	HOH1101

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 228

Chain	Residue
D	HIS86
D	HIS88
D	HIS149
D	ASP168
D	HOH265
D	HOH640

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 229

Chain	Residue
D	ASP90
D	ASP168
D	HIS210
D	HOH640
D	HOH968

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 230

Chain	Residue
D	ASN162
D	ASN202
D	HOH309
D	HOH1270

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY D 231

Chain	Residue
D	LYS139
D	GLN160
D	HOH1399

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY D 232

Chain	Residue
D	ASP60
D	ASP61
D	LYS62
D	HOH317

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE83-GLY102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
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	HIS86
D	HIS86
D	HIS88
D	HIS149
A	HIS88
A	HIS149
B	HIS86
B	HIS88
B	HIS149
C	HIS86
C	HIS88
C	HIS149

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:20677753, ECO:0000269\|PubMed:24059435, ECO:0000269\|PubMed:26482303

Chain	Residue	Details
A	ASP90
D	ASP90
D	ASP168
D	HIS210
A	ASP168
A	HIS210
B	ASP90
B	ASP168
B	HIS210
C	ASP90
C	ASP168
C	HIS210

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:26482303

Chain	Residue	Details
A	LYS171
B	LYS171
C	LYS171
D	LYS171

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:26482303, ECO:0000269\|PubMed:9761898

Chain	Residue	Details
A	ASN180
B	ASN180
C	ASN180
D	ASN180

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
A	HIS86	metal ligand
A	HIS88	metal ligand
A	ASP90	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS149	metal ligand
A	ASN180	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
B	HIS86	metal ligand
B	HIS88	metal ligand
B	ASP90	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS149	metal ligand
B	ASN180	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
C	HIS86	metal ligand
C	HIS88	metal ligand
C	ASP90	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS149	metal ligand
C	ASN180	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
D	HIS86	metal ligand
D	HIS88	metal ligand
D	ASP90	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS149	metal ligand
D	ASN180	electrostatic stabiliser, hydrogen bond donor

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