Structure of PDB 5kmw Chain A

Receptor sequence
>5kmwA (length=256) Species: 562 (Escherichia coli) [Search protein sequence]
VQQQLEALEKSSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAA
VLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTMTLAELGAAALQY
SDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTAPTLNTAIPGDPRD
TTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPKSW
VVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAENRNDILAA
AAKIVT
3D structure
PDB5kmw TOHO1 Beta lactamase mutant E166A/R274N/R276N -benzyl penicillin complex
ChainA
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S69 K72 S129 A165 K233 S236
Catalytic site (residue number reindexed from 1) S41 K44 S101 A137 K205 S208
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 PNM A S69 S129 N169 T234 G235 S236 S41 S101 N141 T206 G207 S208
BS02 PNN A N103 Y104 N75 Y76
BS03 PNN A N103 P166 N169 D238 N75 P138 N141 D210
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:5kmw, PDBe:5kmw, PDBj:5kmw
PDBsum5kmw
PubMed
UniProtQ47066|BLT1_ECOLX Beta-lactamase Toho-1 (Gene Name=bla)

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