5JMX

Crystal Structure of BcII metallo-beta-lactamase in complex with DZ-305

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	4
Details	binding site for residue ZN A 301

Chain	Residue
A	ASP120
A	CYS198
A	HIS240
A	DZ5304

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 302

Chain	Residue
A	HIS116
A	HIS118
A	HIS179
A	DZ5304

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 303

Chain	Residue
A	LYS169
A	GLN190
A	HOH506
A	LYS103

---

site_id	AC4
Number of Residues	11
Details	binding site for residue DZ5 A 304

Chain	Residue
A	HIS118
A	ASP120
A	HIS179
A	CYS198
A	ASN210
A	ASP213
A	HIS240
A	ZN301
A	ZN302
A	HOH437
A	HOH448

---

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 305

Chain	Residue
A	THR59
A	ASN72
A	GLY241
A	GLU242
A	VAL243

---

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 306

Chain	Residue
A	ALA117
A	ASN148
A	THR180
A	ASP182
A	ASP213

---

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL A 307

Chain	Residue
A	GLU99
A	GLU130
A	ARG131
A	HOH493
A	HOH496
A	HOH527

---

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	ASN210	electrostatic stabiliser, hydrogen bond donor

---