4C1C

Crystal structure of the metallo-beta-lactamase BCII with D-captopril

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	5
Details	BINDING SITE FOR RESIDUE GOL A 1258

Chain	Residue
A	LYS95
A	GLU130
A	ARG131
A	HOH2065
A	HOH2267

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1259

Chain	Residue
A	HOH2094
A	HOH2177
A	HOH2210
A	HOH2268
A	ALA117
A	ASN148
A	THR180
A	ASP182

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1260

Chain	Residue
A	LYS103
A	LYS169
A	GLN190
A	HOH2183

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MCO A 1261

Chain	Residue
A	HIS118
A	ASP120
A	HIS179
A	LYS201
A	LEU208
A	GLY209
A	ASN210
A	HIS240
A	ZN1262
A	ZN1263
A	HOH2091
A	HOH2173
A	HOH2188

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1262

Chain	Residue
A	ASP120
A	CYS198
A	HIS240
A	MCO1261
A	HOH2091

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1263

Chain	Residue
A	HIS116
A	HIS118
A	HIS179
A	MCO1261
A	HOH2091

---

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

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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	ASN210	electrostatic stabiliser, hydrogen bond donor

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