Structure of PDB 6mll Chain A

Receptor sequence
>6mllA (length=268) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SHMLTNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSF
KGFLAAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAEL
SAAAVQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSA
IPGDARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIR
AAVPADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDK
HSEAVIAAAARLALEGLG
3D structure
PDB6mll Active-Site Druggability of Carbapenemases and Broad-Spectrum Inhibitor Discovery.
ChainA
Resolution1.86 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) S48 K51 S108 E144 K212 T215
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 N1G A S70 P104 S130 L167 N170 T235 G236 T237 C238 S48 P82 S108 L145 N148 T213 G214 T215 C216 MOAD: Ki=239uM
PDBbind-CN: -logKd/Ki=3.62,Ki=239uM
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:6mll, PDBe:6mll, PDBj:6mll
PDBsum6mll
PubMed30942078
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

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