Structure of PDB 3fkv Chain A

Receptor sequence
>3fkvA (length=356) Species: 562 (Escherichia coli) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSRTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSKIALAARPVKAITPPT
PAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQ
ILNALQ
3D structure
PDB3fkv Re-examining the role of Lys67 in class C beta-lactamase catalysis.
ChainA
Resolution1.847 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 R67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 R64 Y109 A111 V118 Y147 G153 E269 K310 A313
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 BZB A S64 R67 Y150 N152 Y221 A318 S61 R64 Y147 N149 Y218 A313 PDBbind-CN: -logKd/Ki=7.57,Ki=0.027uM
BindingDB: IC50=200nM,Ki=27nM
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: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:3fkv, PDBe:3fkv, PDBj:3fkv
PDBsum3fkv
PubMed19241376
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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