Structure of PDB 5eec Chain B

Receptor sequence
>5eecB (length=265) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
LTNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFKGF
LAAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELSAA
AVQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAIPG
DARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRAAV
PADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKHSE
AVIAAAARLALEGLG
3D structure
PDB5eec Crystal Structures of KPC-2 and SHV-1 beta-Lactamases in Complex with the Boronic Acid Transition State Analog S02030.
ChainB
Resolution1.87 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 ZXM B S70 W105 S130 N132 E166 L167 N170 T235 G236 T237 C238 S45 W80 S105 N107 E141 L142 N145 T210 G211 T212 C213
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:5eec, PDBe:5eec, PDBj:5eec
PDBsum5eec
PubMed26729491
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

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