Structure of PDB 6d15 Chain A

Receptor sequence
>6d15A (length=270) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
HMLTNLVAEPFAKLEQDFGGSIGVYAMDTGSGATVSYRAEERFPLCSSFK
GFLAAAVLARSQQQAGLLDTPIRYGKNALVPWSPISEKYLTTGMTVAELS
AAAVQYSDNAAANLLLKELGGPAGLTAFMRSIGDTTFRLDRWELELNSAI
PGDARDTSSPRAVTESLQKLTLGSALAAPQRQQFVDWLKGNTTGNHRIRA
AVPADWAVGDKTGTCGVYGTANDYAVVWPTGRAPIVLAVYTRAPNKDDKH
SEAVIAAAARLALEGLGVNG
3D structure
PDB6d15 Heteroaryl Phosphonates as Noncovalent Inhibitors of Both Serine- and Metallocarbapenemases.
ChainA
Resolution1.3 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) S47 K50 S107 E143 K211 T214
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 TWB A S70 S130 T235 G236 T237 S47 S107 T212 G213 T214 MOAD: Ki=32.9uM
PDBbind-CN: -logKd/Ki=4.48,Ki=32.9uM
BS02 TWB A R83 G147 A150 F151 S154 R60 G124 A127 F128 S131 MOAD: Ki=32.9uM
PDBbind-CN: -logKd/Ki=4.48,Ki=32.9uM
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:6d15, PDBe:6d15, PDBj:6d15
PDBsum6d15
PubMed31483651
UniProtQ9F663|BLKPC_KLEPN Carbapenem-hydrolyzing beta-lactamase KPC (Gene Name=bla)

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