8Z5L

Crystal structure of metallo-beta-lactamse, IMP-1, complexed with a quinolinone-based inhibitor

This is a non-PDB format compatible entry.

Replaces:  8Y0S

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0017001	biological_process	antibiotic catabolic process
A	0042597	cellular_component	periplasmic space
B	0008270	molecular_function	zinc ion binding
B	0008800	molecular_function	beta-lactamase activity
B	0017001	biological_process	antibiotic catabolic process
B	0042597	cellular_component	periplasmic space
C	0008270	molecular_function	zinc ion binding
C	0008800	molecular_function	beta-lactamase activity
C	0017001	biological_process	antibiotic catabolic process
C	0042597	cellular_component	periplasmic space
D	0008270	molecular_function	zinc ion binding
D	0008800	molecular_function	beta-lactamase activity
D	0017001	biological_process	antibiotic catabolic process
D	0042597	cellular_component	periplasmic space

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE78-SER97

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

Chain	Residue	Details
A	PRO153-LYS165

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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