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1YSB

Yeast Cytosine Deaminase Triple Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004131molecular_functioncytosine deaminase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0008655biological_processpyrimidine-containing compound salvage
A0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A0016787molecular_functionhydrolase activity
A0019858biological_processcytosine metabolic process
A0044206biological_processUMP salvage
A0046087biological_processcytidine metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004131molecular_functioncytosine deaminase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0008655biological_processpyrimidine-containing compound salvage
B0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B0016787molecular_functionhydrolase activity
B0019858biological_processcytosine metabolic process
B0044206biological_processUMP salvage
B0046087biological_processcytidine metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 500
ChainResidue
BHIS262
BCYS291
BCYS294
BZN502
BHOH1332

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHOH1335
AHIS62
ACYS91
ACYS94
AZN503

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BGLU264
BZN500
BHOH1054
BHOH1331
BHOH1332
BHOH1333

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AGLU64
AZN501
AHOH1044
AHOH1334
AHOH1335
AHOH1336

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BGLY326
BASP346
BHOH1026
BHOH1065
BHOH1071

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 Residues240
DetailsDomain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12637534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UAQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding 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"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1uaq
ChainResidueDetails
AGLU64
ACYS91
ASER89

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1uaq
ChainResidueDetails
BGLU264
BCYS291
BSER289

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
BHIS262metal ligand
BGLU264proton acceptor, proton donor
BSER289electrostatic stabiliser
BCYS291metal ligand
BCYS294metal ligand

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PDB entries from 2025-10-15

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