Structure of PDB 4x6t Chain A

Receptor sequence
>4x6tA (length=265) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
ALADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVA
AVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVATGMTIGQLCDAAIRYS
DGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELARDPPGD
ERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP
ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPRE
ALLAEAATCVAGVLA
3D structure
PDB4x6t Inhibiting the beta-Lactamase of Mycobacterium tuberculosis (Mtb) with Novel Boronic Acid Transition-State Inhibitors (BATSIs).
ChainA
Resolution1.4 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 E182 K250 T253
Catalytic site (residue number reindexed from 1) S42 K45 S100 E140 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 3Y6 A C83 S84 R115 S116 I117 S142 E182 P183 R187 T253 G254 D255 C41 S42 R73 S74 I75 S100 E140 P141 R145 T211 G212 D213
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4x6t, PDBe:4x6t, PDBj:4x6t
PDBsum4x6t
PubMed27622739
UniProtP9WKD3|BLAC_MYCTU Beta-lactamase (Gene Name=blaC)

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