5FQA

Crystal Structure of Bacillus cereus Metallo-Beta-Lactamase 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE A 258

Chain	Residue
A	HIS116
A	HIS118
A	HIS179
A	CSD198
A	FE259
A	OH263
A	HOH2144

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE A 259

Chain	Residue
A	HIS240
A	FE258
A	OH263
A	HOH2244
A	ASP120
A	CSD198

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 260

Chain	Residue
A	LYS95
A	GLU130
A	ARG131
A	HOH2081
A	HOH2099
A	HOH2350

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 262

Chain	Residue
A	LYS103
A	LYS169
A	GLN190
A	HOH2352
A	HOH2353

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OH A 263

Chain	Residue
A	HIS116
A	HIS118
A	ASP120
A	HIS179
A	CSD198
A	FE258
A	FE259
A	HOH2144
A	HOH2244

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 264

Chain	Residue
A	HIS118
A	ASN148
A	HOH2140
A	HOH2192
A	HOH2285

---

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	ILE113-GLY132

---

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

Chain	Residue	Details
A	PRO189-LYS201

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
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	3
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	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
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	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	HIS179	metal ligand
A	ALA214	electrostatic stabiliser, hydrogen bond donor

---