Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8I3N

crystal structure of yeast cytosine deaminase mutant yCD-RQ

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	0016814	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A	0019239	molecular_function	deaminase activity
A	0019858	biological_process	cytosine metabolic process
A	0034654	biological_process	nucleobase-containing compound biosynthetic 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	0016814	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
B	0019239	molecular_function	deaminase activity
B	0019858	biological_process	cytosine metabolic process
B	0034654	biological_process	nucleobase-containing compound biosynthetic process
B	0044206	biological_process	UMP salvage
B	0046087	biological_process	cytidine metabolic process
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004131	molecular_function	cytosine deaminase activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0008270	molecular_function	zinc ion binding
C	0008655	biological_process	pyrimidine-containing compound salvage
C	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
C	0016787	molecular_function	hydrolase activity
C	0016814	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
C	0019239	molecular_function	deaminase activity
C	0019858	biological_process	cytosine metabolic process
C	0034654	biological_process	nucleobase-containing compound biosynthetic process
C	0044206	biological_process	UMP salvage
C	0046087	biological_process	cytidine metabolic process
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004131	molecular_function	cytosine deaminase activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0008270	molecular_function	zinc ion binding
D	0008655	biological_process	pyrimidine-containing compound salvage
D	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
D	0016787	molecular_function	hydrolase activity
D	0016814	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
D	0019239	molecular_function	deaminase activity
D	0019858	biological_process	cytosine metabolic process
D	0034654	biological_process	nucleobase-containing compound biosynthetic process
D	0044206	biological_process	UMP salvage
D	0046087	biological_process	cytidine metabolic process
D	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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:12637534, ECO:0007744\|PDB:1UAQ

Chain	Residue	Details
A	GLU64
B	GLU64
C	GLU64
D	GLU64

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:12637534, ECO:0000269\|PubMed:12906827, ECO:0007744\|PDB:1P6O, ECO:0007744\|PDB:1UAQ

Chain	Residue	Details
A	ASN51
A	ASP155
B	ASN51
B	ASP155
C	ASN51
C	ASP155
D	ASN51
D	ASP155

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:12637534, ECO:0000269\|PubMed:12906827, ECO:0000269\|PubMed:15879217, ECO:0007744\|PDB:1OX7, ECO:0007744\|PDB:1P6O, ECO:0007744\|PDB:1RB7, ECO:0007744\|PDB:1UAQ, ECO:0007744\|PDB:1YSB, ECO:0007744\|PDB:1YSD

Chain	Residue	Details
A	HIS62
D	HIS62
D	CYS91
D	CYS94
A	CYS91
A	CYS94
B	HIS62
B	CYS91
B	CYS94
C	HIS62
C	CYS91
C	CYS94

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

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

site_id	MCSA3
Number of Residues	5
Details	M-CSA 636

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

site_id	MCSA4
Number of Residues	5
Details	M-CSA 636

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)