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8I3O

crystal structure of yeast cytosine deaminase mutant yCD-RQ-1/8SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004131molecular_functioncytosine deaminase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0008270molecular_functionzinc ion binding
A0008655biological_processpyrimidine-containing compound salvage
A0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A0016787molecular_functionhydrolase activity
A0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A0019239molecular_functiondeaminase activity
A0019858biological_processcytosine metabolic process
A0044206biological_processUMP salvage
A0046087biological_processcytidine metabolic process
A0046872molecular_functionmetal ion binding
A0102480molecular_function5-fluorocytosine deaminase activity
B0004131molecular_functioncytosine deaminase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0008270molecular_functionzinc ion binding
B0008655biological_processpyrimidine-containing compound salvage
B0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B0016787molecular_functionhydrolase activity
B0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
B0019239molecular_functiondeaminase activity
B0019858biological_processcytosine metabolic process
B0044206biological_processUMP salvage
B0046087biological_processcytidine metabolic process
B0046872molecular_functionmetal ion binding
B0102480molecular_function5-fluorocytosine deaminase activity
C0004131molecular_functioncytosine deaminase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006139biological_processnucleobase-containing compound metabolic process
C0008270molecular_functionzinc ion binding
C0008655biological_processpyrimidine-containing compound salvage
C0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
C0016787molecular_functionhydrolase activity
C0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
C0019239molecular_functiondeaminase activity
C0019858biological_processcytosine metabolic process
C0044206biological_processUMP salvage
C0046087biological_processcytidine metabolic process
C0046872molecular_functionmetal ion binding
C0102480molecular_function5-fluorocytosine deaminase activity
D0004131molecular_functioncytosine deaminase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0006139biological_processnucleobase-containing compound metabolic process
D0008270molecular_functionzinc ion binding
D0008655biological_processpyrimidine-containing compound salvage
D0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
D0016787molecular_functionhydrolase activity
D0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
D0019239molecular_functiondeaminase activity
D0019858biological_processcytosine metabolic process
D0044206biological_processUMP salvage
D0046087biological_processcytidine metabolic process
D0046872molecular_functionmetal ion binding
D0102480molecular_function5-fluorocytosine deaminase activity
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues37
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HGEisTLencgrlegkvykdttlyttls............PCdm......CtgaI
ChainResidueDetails
AHIS62-ILE98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ
ChainResidueDetails
AGLU64
BGLU64
CGLU64
DGLU64

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
ChainResidueDetails
AASN51
AASP155
BASN51
BASP155
CASN51
CASP155
DASN51
DASP155

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: 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
ChainResidueDetails
AHIS62
ACYS91
ACYS94
BHIS62
BCYS91
BCYS94
CHIS62
CCYS91
CCYS94
DHIS62
DCYS91
DCYS94

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
AHIS62metal ligand
AGLU64proton acceptor, proton donor
ASER89electrostatic stabiliser
ACYS91metal ligand
ACYS94metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
BHIS62metal ligand
BGLU64proton acceptor, proton donor
BSER89electrostatic stabiliser
BCYS91metal ligand
BCYS94metal ligand

site_idMCSA3
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
CHIS62metal ligand
CGLU64proton acceptor, proton donor
CSER89electrostatic stabiliser
CCYS91metal ligand
CCYS94metal ligand

site_idMCSA4
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
DHIS62metal ligand
DGLU64proton acceptor, proton donor
DSER89electrostatic stabiliser
DCYS91metal ligand
DCYS94metal ligand

221051

PDB entries from 2024-06-12

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