eF-site ID 1ysb-AB PDB Code 1ysb Chain A, B click to enlarge Title Yeast Cytosine Deaminase Triple Mutant Classification HYDROLASE Compound Cytosine deaminase Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FCY1_YEAST) Sequence A:  TGGMASKWDQKGMDIAYEEALLGYKEGGVPIGGCLINNKD GSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDT TLYTTLSPCDMCTGAIIMYGIPRCVIGENVNFKSKGEKYL QTRGHEVVVVDDERCKKLMKQFIDERPQDWFEDIGE B:  GSSMVTGGMASKWDQKGMDIAYEEALLGYKEGGVPIGGCL INNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK VYKDTTLYTTLSPCDMCTGAIIMYGIPRCVIGENVNFKSK GEKYLQTRGHEVVVVDDERCKKLMKQFIDERPQDWFEDIG E Description Functional site 1) chain B residue 262 type sequence H description BINDING SITE FOR RESIDUE ZN B 500 source : AC1 2) chain B residue 291 type sequence C description BINDING SITE FOR RESIDUE ZN B 500 source : AC1 3) chain B residue 294 type sequence C description BINDING SITE FOR RESIDUE ZN B 500 source : AC1 4) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 5) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 6) chain A residue 94 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 7) chain B residue 264 type sequence E description BINDING SITE FOR RESIDUE ZN B 502 source : AC3 8) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE ZN A 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 62 type catalytic sequence H description 636 source MCSA : MCSA1 12) chain A residue 64 type catalytic sequence E description 636 source MCSA : MCSA1 13) chain A residue 89 type catalytic sequence S description 636 source MCSA : MCSA1 14) chain A residue 91 type catalytic sequence C description 636 source MCSA : MCSA1 15) chain A residue 94 type catalytic sequence C description 636 source MCSA : MCSA1 16) chain B residue 262 type catalytic sequence H description 636 source MCSA : MCSA2 17) chain B residue 264 type catalytic sequence E description 636 source MCSA : MCSA2 18) chain B residue 289 type catalytic sequence S description 636 source MCSA : MCSA2 19) chain B residue 291 type catalytic sequence C description 636 source MCSA : MCSA2 20) chain B residue 294 type catalytic sequence C description 636 source MCSA : MCSA2 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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

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