Structure of PDB 4lv3 Chain A

Receptor sequence
>4lv3A (length=352) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIKIALAARPVKAITPPTPAVR
ASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNA
LQ
3D structure
PDB4lv3 Covalent docking of large libraries for the discovery of chemical probes.
ChainA
Resolution1.42 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K306 A309
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 25N A S64 Q120 Y150 N152 Y221 G317 A318 S61 Q117 Y147 N149 Y218 G308 A309 PDBbind-CN: -logKd/Ki=5.49,Ki=3.2uM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lv3, PDBe:4lv3, PDBj:4lv3
PDBsum4lv3
PubMed25344815
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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