5FQB

Crystal Structure of Bacillus cereus Metallo-Beta-Lactamase with 2C

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 295

Chain	Residue
A	ASP123
A	CYS224
A	HIS266
A	OK3297

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 296

Chain	Residue
A	HIS119
A	HIS121
A	HIS199
A	OK3297

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE OK3 A 297

Chain	Residue
A	TRP90
A	HIS119
A	HIS121
A	ALA122
A	ASP123
A	HIS199
A	CYS224
A	LYS227
A	ASN236
A	ASP239
A	HIS266
A	ZN295
A	ZN296
A	HOH2120
A	HOH2132
A	HOH2150
A	PHE65

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 298

Chain	Residue
A	LYS105
A	LYS189
A	GLN213
A	HOH2126

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 299

Chain	Residue
A	GLU100
A	GLU133
A	ARG134
A	HOH2190

---

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	ILE116-GLY136

---

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

Chain	Residue	Details
A	PRO212-LYS227

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
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	HIS119
A	HIS121
A	HIS199

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303

Chain	Residue	Details
A	ASP123
A	CYS224
A	HIS266

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26482303

Chain	Residue	Details
A	LYS227

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:9761898

Chain	Residue	Details
A	ASN236

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 16

Chain	Residue	Details
A	HIS119	metal ligand
A	HIS121	metal ligand
A	ASP123	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS199	metal ligand
A	ASN236	electrostatic stabiliser, hydrogen bond donor

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