7ZO6

L1 metallo-beta-lactamase in complex with hydrolysed cefoxitin

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 PROSITE/UniProt

site_id	PS00743
Number of Residues	21
Details	BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG

Chain	Residue	Details
A	LEU81-GLY101

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 258

Chain	Residue	Details
A	HIS84	metal ligand
A	HIS86	metal ligand
A	ASP88	metal ligand
A	HIS89	metal ligand
A	HIS160	metal ligand
A	TYR191	electrostatic stabiliser, hydrogen bond donor
A	HIS225	metal ligand

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