Structure of PDB 6ooe Chain B

Receptor sequence
>6ooeB (length=261) Species: 562 (Escherichia coli) [Search protein sequence]
SAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAA
AAVLKQSETQKQLLNQPVEIKHADLVNYNPIAEKHVNGTMTLAELSAAAL
QYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP
RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPT
SWTVGDKTGSGGYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVL
ASAARIIAEGL
3D structure
PDB6ooe An Empirical Study of Amide-Heteroarene pi-Stacking Interactions Using Reversible Inhibitors of a Bacterial Serine Hydrolase.
ChainB
Resolution1.26 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) S43 K46 S103 E139 K207 S210
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 R6Z B N104 Y105 T216 S237 S274 R276 N77 Y78 T189 S210 S245 R247 MOAD: Kd=0.292uM
BS02 R6Z B N104 Y105 S130 N132 P167 N170 T171 T235 G236 S237 G238 G240 N77 Y78 S103 N105 P140 N143 T144 T208 G209 S210 G211 G212 MOAD: Kd=0.292uM
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:6ooe, PDBe:6ooe, PDBj:6ooe
PDBsum6ooe
PubMed32774871
UniProtI7AP60

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