Structure of PDB 6ooj Chain A

Receptor sequence
>6oojA (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
PTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
3D structure
PDB6ooj An Empirical Study of Amide-Heteroarene pi-Stacking Interactions Using Reversible Inhibitors of a Bacterial Serine Hydrolase.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 J1X A N104 Y105 T216 S237 S274 N79 Y80 T191 S212 S247 MOAD: Kd=19.4uM
BS02 J1X A N104 Y105 S130 N132 P167 N170 T171 T235 G236 S237 G238 D240 N79 Y80 S105 N107 P142 N145 T146 T210 G211 S212 G213 D214 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6ooj, PDBe:6ooj, PDBj:6ooj
PDBsum6ooj
PubMed32774871
UniProtQ9L5C7

[Back to BioLiP]