Structure of PDB 4r88 Chain B

Receptor sequence
>4r88B (length=413) Species: 1420012 (Klebsiella pneumoniae 30660/NJST258_1) [Search protein sequence]
MKIINARLRRQEALFTLDLQDGIIHRITAQAAMQTADAGAIDAQGRLAIP
PFVEPHIHLDATLTAGEPEWNRSGTLFEGITRWSQRKASITPEDTRQRAL
KTIGMLRDFGVQHVRTHVDVTDPSLAALQALLAVKQEAADLIDLQIVAFP
QEGIESYPNGRELMTRAIEMGADVVGGIPHYENTRDKGVSSVMFLMDLAQ
RYGRLVDVHCDEIDDPQSRFLEVLAEEARVRGMGAQVTASHTCAMGSYDN
AYCSKLFRLLKASGINFISCPTESIHLQGRFDSWPKRRGVTRVAELDRAG
INVCFAQDSIQDPWYPLGNGNILRILDAGLHICHMLGYDDLQRCLDFVTD
NSARALCLGDNYGLAEGRPANLLILDAENDYEAVRRQARVLTSIRHGKVI
LQREVEHIRYPAN
3D structure
PDB4r88 Crystal structure of 5-methylcytosine deaminase from Klebsiella pneumoniae liganded with 5-fluorocytosine
ChainB
Resolution1.952 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H56 H58 Q151 H209 E212 D308
Catalytic site (residue number reindexed from 1) H56 H58 Q151 H209 E212 D308
Enzyme Commision number 3.5.4.1: cytosine deaminase.
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 1LD B H58 L76 Q151 E212 E273 W314 H58 L76 Q151 E212 E273 W314
BS02 FE2 B H56 H58 H209 H241 D308 H56 H58 H209 H241 D308
Gene Ontology
Molecular Function
GO:0004131 cytosine deaminase activity
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0035888 isoguanine deaminase activity
GO:0046872 metal ion binding
Biological Process
GO:0006209 cytosine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4r88, PDBe:4r88, PDBj:4r88
PDBsum4r88
PubMed
UniProtA0A0E1CHI1

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