2NXA

Structure of Zn-dependent Metallo-Beta-Lactamase from Bacillus Cereus R121H, C221D Double Mutant

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	HIS86
A	HIS88
A	HIS149
A	ASP168

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE83-GLY102

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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	HIS86
A	HIS149
A	HIS88

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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	ASP168
A	HIS210
A	ASP90

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

Chain	Residue	Details
A	LYS171

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

Chain	Residue	Details
A	ASN180

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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

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