Structure of PDB 6qwb Chain A

Receptor sequence
>6qwbA (length=268) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
LTNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGF
LAAAVLARSQQQAGLLDTPIRYGKNALVRWSPISEKYLTTGMTVAELSAA
AVQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPG
DARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAV
PADWAVGDKTGTCGGYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHSE
AVIAAAARLALEGLGVNG
3D structure
PDB6qwb Molecular Basis of Class A beta-Lactamase Inhibition by Relebactam.
ChainA
Resolution1.04 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) S45 K48 S105 E141 K209 T212
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 JJT A S70 W105 S130 N132 G236 T237 S45 W80 S105 N107 G211 T212
BS02 MK7 A S70 W105 S130 T235 G236 T237 S45 W80 S105 T210 G211 T212 PDBbind-CN: -logKd/Ki=6.04,IC50=910nM
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:6qwb, PDBe:6qwb, PDBj:6qwb
PDBsum6qwb
PubMed31383664
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

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