Structure of PDB 3g77 Chain A

Receptor sequence

>3g77A (length=423) Species: 83333 (Escherichia coli K-12)

ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITENSLDAEQGLV
IPPFVEPHIHLDTTQTAGQPNWNQSGTLFEGIERWAERKALLTHDDVKQR
AWQTLKWQIANGIQHVRTHVDVSDATLTALKAMLEVKQEVAPWIDLQIAA
FPQEGILSYPNGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL
AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVTASHTTAMHSY
NGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLE
SGINVCFGHDDVCGPWYPLGTANMLQVLHMGLHVCQLMGYGQINDGLNLI
THHSARTLNLQDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV
IASTQPAQTTVYLEQPEAIDYKR

3D structure

• PDB: 3g77 Bacterial cytosine deaminase mutants created by molecular engineering show improved 5-fluorocytosine-mediated cell killing in vitro and in vivo.
• Chain: A
• Resolution: 1.8 Å

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

External links

• PDB: RCSB:3g77, PDBe:3g77, PDBj:3g77
• PDBsum: 3g77
• PubMed: 19487291
• UniProt: P25524|CODA_ECOLI Cytosine deaminase (Gene Name=codA)