8VLJ

Crystal structure of the cacodylate-bound yeast cytosine deaminase (closed form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004131	molecular_function	cytosine deaminase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0008270	molecular_function	zinc ion binding
A	0008655	biological_process	pyrimidine-containing compound salvage
A	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A	0016787	molecular_function	hydrolase activity
A	0019858	biological_process	cytosine metabolic process
A	0044206	biological_process	UMP salvage
A	0046087	biological_process	cytidine metabolic process
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004131	molecular_function	cytosine deaminase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0008270	molecular_function	zinc ion binding
B	0008655	biological_process	pyrimidine-containing compound salvage
B	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B	0016787	molecular_function	hydrolase activity
B	0019858	biological_process	cytosine metabolic process
B	0044206	biological_process	UMP salvage
B	0046087	biological_process	cytidine metabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00903
Number of Residues	37
Details	CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HGEisTLencgrlegkvykdttlyttls............PCdm......CtgaI

Chain	Residue	Details
A	HIS62-ILE98

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	Domain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906827","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P6O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12906827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15879217","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OX7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P6O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RB7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YSB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YSD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 636

Chain	Residue	Details
A	HIS62	metal ligand
A	GLU64	proton acceptor, proton donor
A	SER89	electrostatic stabiliser
A	CYS91	metal ligand
A	CYS94	metal ligand

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 636

Chain	Residue	Details
B	HIS62	metal ligand
B	GLU64	proton acceptor, proton donor
B	SER89	electrostatic stabiliser
B	CYS91	metal ligand
B	CYS94	metal ligand

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