Structure of PDB 5ll7 Chain A

Receptor sequence
>5ll7A (length=264) Species: 562 (Escherichia coli) [Search protein sequence]
TNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGFL
AAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELSAAA
VQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPGD
ARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAVP
ADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHSEA
VIAAAARLALEGLG
3D structure
PDB5ll7 Phenylboronic Acid Derivatives as Validated Leads Active in Clinical Strains Overexpressing KPC-2: A Step against Bacterial Resistance.
ChainA
Resolution1.4 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 6YV A C69 S70 W105 S130 E166 N170 T235 T237 C43 S44 W79 S104 E140 N144 T209 T211 PDBbind-CN: -logKd/Ki=5.61,Ki=2.43uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase 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:5ll7, PDBe:5ll7, PDBj:5ll7
PDBsum5ll7
PubMed29356380
UniProtA0A0H4IUK8

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