6YI4

Structure of IMP-13 metallo-beta-lactamase complexed with citrate anion

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0008270	molecular_function	zinc ion binding
AAA	0008800	molecular_function	beta-lactamase activity
AAA	0016787	molecular_function	hydrolase activity
AAA	0017001	biological_process	antibiotic catabolic process
AAA	0042597	cellular_component	periplasmic space
AAA	0046677	biological_process	response to antibiotic
AAA	0046872	molecular_function	metal ion binding
BBB	0008270	molecular_function	zinc ion binding
BBB	0008800	molecular_function	beta-lactamase activity
BBB	0016787	molecular_function	hydrolase activity
BBB	0017001	biological_process	antibiotic catabolic process
BBB	0042597	cellular_component	periplasmic space
BBB	0046677	biological_process	response to antibiotic
BBB	0046872	molecular_function	metal ion binding
CCC	0008270	molecular_function	zinc ion binding
CCC	0008800	molecular_function	beta-lactamase activity
CCC	0016787	molecular_function	hydrolase activity
CCC	0017001	biological_process	antibiotic catabolic process
CCC	0042597	cellular_component	periplasmic space
CCC	0046677	biological_process	response to antibiotic
CCC	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
AAA	ILE74-SER93

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

Chain	Residue	Details
AAA	PRO149-LYS161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:32205343, ECO:0000269\|Ref.11, ECO:0007744\|PDB:6R73, ECO:0007744\|PDB:6R79, ECO:0007744\|PDB:6RZR, ECO:0007744\|PDB:6RZS, ECO:0007744\|PDB:6S0H, ECO:0007744\|PDB:6YI4

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P52699