Structure of PDB 5top Chain A

Receptor sequence
>5topA (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCGTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
3D structure
PDB5top Mechanisms of proton relay and product release by Class A beta-lactamase at ultrahigh resolution.
ChainA
Resolution1.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) G45 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 JSE A G70 K73 N104 S130 P167 N170 T171 T235 G236 S237 D240 G45 K48 N79 S105 P142 N145 T146 T210 G211 S212 D214
BS02 JSC A K82 Q192 H197 A198 K57 Q167 H172 A173
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:5top, PDBe:5top, PDBj:5top
PDBsum5top
PubMed29095570
UniProtH6UQI0

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