Structure of PDB 6mey Chain A

Receptor sequence
>6meyA (length=263) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
VAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGFLAAA
VLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELSAAAVQY
SDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPGDARD
TSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAVPADW
AVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHEAVIAA
AARLALEGLGVNG
3D structure
PDB6mey Active-Site Druggability of Carbapenemases and Broad-Spectrum Inhibitor Discovery.
ChainA
Resolution1.42 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) S41 K44 S101 E137 K205 T208
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 O5E A P94 T115 P65 T86 MOAD: Ki=479uM
PDBbind-CN: -logKd/Ki=3.32,Ki=479uM
BS02 O5E A S84 Q85 Q87 A88 G89 L90 L91 A200 S55 Q56 Q58 A59 G60 L61 L62 A171 MOAD: Ki=479uM
PDBbind-CN: -logKd/Ki=3.32,Ki=479uM
BS03 O5E A S70 S130 N170 T235 G236 T237 S41 S101 N141 T206 G207 T208 MOAD: Ki=479uM
PDBbind-CN: -logKd/Ki=3.32,Ki=479uM
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:6mey, PDBe:6mey, PDBj:6mey
PDBsum6mey
PubMed30942078
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

[Back to BioLiP]