8ECF

Cryo structure of Mycobacterium tuberculosis beta lactamase microcrystals mixed with sulbactam for 3 hours

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005886	cellular_component	plasma membrane
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030655	biological_process	beta-lactam antibiotic catabolic process
A	0033250	molecular_function	penicillinase activity
A	0033251	molecular_function	cephalosporinase activity
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
B	0005576	cellular_component	extracellular region
B	0005886	cellular_component	plasma membrane
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030655	biological_process	beta-lactam antibiotic catabolic process
B	0033250	molecular_function	penicillinase activity
B	0033251	molecular_function	cephalosporinase activity
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
C	0005576	cellular_component	extracellular region
C	0005886	cellular_component	plasma membrane
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0030655	biological_process	beta-lactam antibiotic catabolic process
C	0033250	molecular_function	penicillinase activity
C	0033251	molecular_function	cephalosporinase activity
C	0042597	cellular_component	periplasmic space
C	0046677	biological_process	response to antibiotic
D	0005576	cellular_component	extracellular region
D	0005886	cellular_component	plasma membrane
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0030655	biological_process	beta-lactam antibiotic catabolic process
D	0033250	molecular_function	penicillinase activity
D	0033251	molecular_function	cephalosporinase activity
D	0042597	cellular_component	periplasmic space
D	0046677	biological_process	response to antibiotic

Functional Information from PROSITE/UniProt

site_id	PS00146
Number of Residues	16
Details	BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL

Chain	Residue	Details
A	PHE66-LEU81

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112

Chain	Residue	Details
A	SER70
B	SER70
C	SER70
D	SER70

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112

Chain	Residue	Details
A	GLU168
B	GLU168
C	GLU168
D	GLU168

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112

Chain	Residue	Details
A	SER128
A	THR237
B	SER128
B	THR237
C	SER128
C	THR237
D	SER128
D	THR237

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112

Chain	Residue	Details
A	LYS73
B	LYS73
C	LYS73
D	LYS73

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site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821

Chain	Residue	Details
A	ILE103
B	ILE103
C	ILE103
D	ILE103

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