Structure of PDB 6jn5 Chain C

Receptor sequence
>6jn5C (length=263) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
TNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGFL
AAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELSAAA
VQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPGD
ARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAVP
ADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHSEA
VIAAAARLALEGL
3D structure
PDB6jn5 Structure-Based Development of (1-(3'-Mercaptopropanamido)methyl)boronic Acid Derived Broad-Spectrum, Dual-Action Inhibitors of Metallo- and Serine-beta-lactamases.
ChainC
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 T237
Catalytic site (residue number reindexed from 1) S44 K47 S104 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 BXU C C69 S70 W105 S130 N132 E166 L167 N170 T237 C43 S44 W79 S104 N106 E140 L141 N144 T211
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6jn5, PDBe:6jn5, PDBj:6jn5
PDBsum6jn5
PubMed31269398
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

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