Structure of PDB 3n8s Chain A

Receptor sequence
>3n8sA (length=265) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVA
AVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVQTGMTIGQLCDAAIRYS
DGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEAPELNRDPPGD
ERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP
ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPRE
ALLAEAATCVAGVLA
3D structure
PDB3n8s Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S84 K87 S142 A182 K250 T253
Catalytic site (residue number reindexed from 1) S42 K45 S100 A140 K208 T211
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 XD2 A S84 I117 S142 N186 T232 T251 G252 T253 G254 S42 I75 S100 N144 T190 T209 G210 T211 G212
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0042597 periplasmic space

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Biological Process
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Cellular Component
External links
PDB RCSB:3n8s, PDBe:3n8s, PDBj:3n8s
PDBsum3n8s
PubMed20961112
UniProtP9WKD3|BLAC_MYCTU Beta-lactamase (Gene Name=blaC)

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