Structure of PDB 6pt5 Chain A

Receptor sequence
>6pt5A (length=245) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
YFQGWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPAS
TFKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVV
PVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQI
SFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIG
WWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP
3D structure
PDB6pt5 Structural Basis for Substrate Specificity and Carbapenemase Activity of OXA-48 Class D beta-Lactamase.
ChainA
Resolution2.304 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 S118 Y123 W157 Y211
Catalytic site (residue number reindexed from 1) S50 K53 S98 Y103 W137 Y191
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 1S7 A S70 S118 V120 L158 T209 G210 Y211 T213 R214 R250 S50 S98 V100 L138 T189 G190 Y191 T193 R194 R230
Gene Ontology
Molecular Function
GO:0008658 penicillin binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
GO:0071555 cell wall organization

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6pt5, PDBe:6pt5, PDBj:6pt5
PDBsum6pt5
PubMed31872762
UniProtQ6XEC0

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