eF-site ID 1ysd-AB PDB Code 1ysd Chain A, B click to enlarge Title Yeast Cytosine Deaminase Double Mutant Classification HYDROLASE Compound Cytosine deaminase Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FCY1_YEAST) Sequence A:  TGGMASKWDQKGMDIAYEEALLGYKEGGVPIGGCLINNKD GSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDT TLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSKGEKYL QTRGHEVVVVDDERCKKLMKQFIDERPQDWFEDIGE B:  GSSMVTGGMASKWDQKGMDIAYEEALLGYKEGGVPIGGCL INNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK VYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSK GEKYLQTRGHEVVVVDDERCKKLMKQFIDERPQDWFEDIG E Description Functional site 1) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 2) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 3) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 4) chain A residue 94 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 5) chain B residue 262 type sequence H description BINDING SITE FOR RESIDUE ZN B 502 source : AC3 6) chain B residue 291 type sequence C description BINDING SITE FOR RESIDUE ZN B 502 source : AC3 7) chain B residue 294 type sequence C description BINDING SITE FOR RESIDUE ZN B 502 source : AC3 8) chain B residue 264 type sequence E description BINDING SITE FOR RESIDUE ZN B 503 source : AC4 9) chain B residue 326 type sequence G description BINDING SITE FOR RESIDUE CA B 504 source : AC5 10) chain B residue 346 type sequence D description BINDING SITE FOR RESIDUE CA B 504 source : AC5 11) chain A residue 64 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI1 12) chain B residue 264 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI1 13) chain A residue 51 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI2 14) chain A residue 155 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI2 15) chain B residue 251 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI2 16) chain B residue 355 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ source Swiss-Prot : SWS_FT_FI2 17) chain A residue 62 type BINDING sequence H description 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 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 91 type BINDING sequence C description 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 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 94 type BINDING sequence C description 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 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 262 type BINDING sequence H description 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 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 291 type BINDING sequence C description 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 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 294 type BINDING sequence C description 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 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 62-98 type prosite sequence HGEISTLENCGRLEGKVYKDTTLYTTLSPCDMCTGAI description CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HGEisTLencgrlegkvykdttlyttls............PCdm......CtgaI source prosite : PS00903 24) chain A residue 62 type catalytic sequence H description 636 source MCSA : MCSA1 25) chain A residue 64 type catalytic sequence E description 636 source MCSA : MCSA1 26) chain A residue 89 type catalytic sequence S description 636 source MCSA : MCSA1 27) chain A residue 91 type catalytic sequence C description 636 source MCSA : MCSA1 28) chain A residue 94 type catalytic sequence C description 636 source MCSA : MCSA1 29) chain B residue 262 type catalytic sequence H description 636 source MCSA : MCSA2 30) chain B residue 264 type catalytic sequence E description 636 source MCSA : MCSA2 31) chain B residue 289 type catalytic sequence S description 636 source MCSA : MCSA2 32) chain B residue 291 type catalytic sequence C description 636 source MCSA : MCSA2 33) chain B residue 294 type catalytic sequence C description 636 source MCSA : MCSA2

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