Structure of PDB 6mnp Chain A

Receptor sequence
>6mnpA (length=266) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
LTNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGF
LAAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELSAA
AVQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPG
DARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAV
PADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHSE
AVIAAAARLALEGLGV
3D structure
PDB6mnp Active-Site Druggability of Carbapenemases and Broad-Spectrum Inhibitor Discovery.
ChainA
Resolution2.202 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 1CE A W105 P107 E110 K111 W80 P82 E85 K86
BS02 1CE A W105 S130 T216 T235 T237 W80 S105 T191 T210 T212
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6mnp, PDBe:6mnp, PDBj:6mnp
PDBsum6mnp
PubMed30942078
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

[Back to BioLiP]