Structure of PDB 4de0 Chain A

Receptor sequence
>4de0A (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
3D structure
PDB4de0 Structure-Based Design of Potent and Ligand-Efficient Inhibitors of CTX-M Class A Beta-Lactamase
ChainA
Resolution1.12 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 S237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 S212
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 0JB A N104 Y105 S130 N132 N170 T235 G236 S237 G238 D240 N79 Y80 S105 N107 N145 T210 G211 S212 G213 D214 MOAD: Ki=1.3uM
PDBbind-CN: -logKd/Ki=5.89,Ki=1.3uM
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:4de0, PDBe:4de0, PDBj:4de0
PDBsum4de0
PubMed22296601
UniProtQ9L5C8

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