Structure of PDB 1fr6 Chain B

Receptor sequence
>1fr6B (length=361) Species: 546 (Citrobacter freundii) [Search protein sequence]
AAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYQGKPYYFTWGKADIAN
NRPVTQQTLFELGSVSKTFNGVLGGDAIARGEIKLSDPVTQYWPELTGKQ
WQGISLLHLATYTAGGLPLQVPDDVTDKAALLRFYQNWQPQWAPGAKRLY
ANSSIGLFGALAVKPSGMSYEEAMSKRVLHPLKLAHTWITVPQSEQKDYA
WGYREGKPVHVSPGQLDAEAYGVKSSVIDMTRWVQANMDASQVQEKTLQQ
GIELAQSRYWRIGDMYQGLGWEMLNWPVKADSIISGSDSKVALAALPAVE
VNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPVRV
EAAWRILEKLQ
3D structure
PDB1fr6 Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis.
ChainB
Resolution2.5 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 G116 P118 V121 Y150 G156 E272 K315 S318
Catalytic site (residue number reindexed from 1) S64 K67 G116 P118 V121 Y150 G156 E272 K315 S318
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 AZR B D123 D124 D123 D124
BS02 AZR B S64 Q120 Y150 Y221 T316 G317 S318 N346 S64 Q120 Y150 Y221 T316 G317 S318 N346
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1fr6, PDBe:1fr6, PDBj:1fr6
PDBsum1fr6
PubMed2300174
UniProtQ46041

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