Structure of PDB 1r9x Chain A

Receptor sequence
>1r9xA (length=423) Species: 562 (Escherichia coli) [Search protein sequence]
ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLV
IPPFVEPHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQR
AWQTLKWQIANGIQHVRTHVDVSDATLTALKAMLEVKQEVAPWIDLQIVA
FPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL
AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVTASHTTAMHSY
NGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLE
SGINVCFGHDGVFDPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLI
THHSARTLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV
IASTQPAQTTVYLEQPEAIDYKR
3D structure
PDB1r9x Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy.
ChainA
Resolution1.58 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H61 H63 Q156 H214 E217 D313
Catalytic site (residue number reindexed from 1) H58 H60 Q153 H211 E214 D310
Enzyme Commision number 3.5.4.-
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 FE A H61 H63 H214 D313 H58 H60 H211 D310
Gene Ontology
Molecular Function
GO:0004131 cytosine deaminase activity
GO:0008198 ferrous iron binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0035888 isoguanine deaminase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006209 cytosine catabolic process
GO:0019858 cytosine metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1r9x, PDBe:1r9x, PDBj:1r9x
PDBsum1r9x
PubMed15381761
UniProtP25524|CODA_ECOLI Cytosine deaminase (Gene Name=codA)

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