Structure of PDB 6bu3 Chain A

Receptor sequence
>6bu3A (length=262) Species: 562 (Escherichia coli) [Search protein sequence]
TSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMA
AAAVLKQSETQKQLLNQPVEIKHADLVNYNPIAEKHVNGTMTLAELSAAA
LQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGD
PRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLP
TSWTVGDKTGSGGYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDV
LASAARIIAEGL
3D structure
PDB6bu3 Antibacterial Spectrum of a Tetrazole-Based Reversible Inhibitor of Serine beta-Lactamases.
ChainA
Resolution1.15 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) S44 K47 S104 E140 K208 S211
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 3GK A N104 Y105 S130 N132 P167 N170 T171 T235 G236 S237 G238 N78 Y79 S104 N106 P141 N144 T145 T209 G210 S211 G212 MOAD: Ki=0.28uM
PDBbind-CN: -logKd/Ki=6.55,Ki=0.28uM
BS02 3GK A N104 Y105 S237 N78 Y79 S211 MOAD: Ki=0.28uM
PDBbind-CN: -logKd/Ki=6.55,Ki=0.28uM
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:6bu3, PDBe:6bu3, PDBj:6bu3
PDBsum6bu3
PubMed29844038
UniProtB5LY47

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