Structure of PDB 4wmc Chain A

Receptor sequence
>4wmcA (length=237) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
EWQENKSWNAHFQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSL
IALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFAR
QIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYH
NKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVEL
DDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP
3D structure
PDB4wmc Molecular Basis of Selective Inhibition and Slow Reversibility of Avibactam against Class D Carbapenemases: A Structure-Guided Study of OXA-24 and OXA-48.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S118 Y123 W157 Y211
Catalytic site (residue number reindexed from 1) S42 K45 S90 Y95 W129 Y183
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 NXL A S70 S118 V120 T209 G210 Y211 R250 S42 S90 V92 T181 G182 Y183 R222 PDBbind-CN: -logKd/Ki=8.05,Kd=9nM
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:4wmc, PDBe:4wmc, PDBj:4wmc
PDBsum4wmc
PubMed25406838
UniProtQ6XEC0

[Back to BioLiP]