Structure of PDB 6ooj Chain B

Receptor sequence
>6oojB (length=260) Species: 562 (Escherichia coli) [Search protein sequence]
AVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAA
AVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAALQ
YSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPR
DTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTS
WTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLA
SAARIIAEGL
3D structure
PDB6ooj An Empirical Study of Amide-Heteroarene pi-Stacking Interactions Using Reversible Inhibitors of a Bacterial Serine Hydrolase.
ChainB
Resolution1.4 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) S42 K45 S102 E138 K206 S209
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 J1X B N104 Y105 T216 S237 S274 R276 N76 Y77 T188 S209 S244 R246 MOAD: Kd=19.4uM
BS02 J1X B N104 Y105 S130 N132 P167 N170 T171 T235 G236 S237 G238 D240 N76 Y77 S102 N104 P139 N142 T143 T207 G208 S209 G210 D211 MOAD: Kd=19.4uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
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:6ooj, PDBe:6ooj, PDBj:6ooj
PDBsum6ooj
PubMed32774871
UniProtQ9L5C7

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