eF-site ID 1p6o-AB PDB Code 1p6o Chain A, B click to enlarge Title The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms. Classification HYDROLASE Compound Cytosine deaminase Source null (FCY1_YEAST) Sequence A:  TGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCLINNKD GSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDT TLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSKGEKYL QTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIGE B:  GSSMVTGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCL INNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK VYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSK GEKYLQTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIG E Description Functional site 1) chain B residue 262 type sequence H description BINDING SITE FOR RESIDUE ZN B 400 source : AC1 2) chain B residue 291 type sequence C description BINDING SITE FOR RESIDUE ZN B 400 source : AC1 3) chain B residue 294 type sequence C description BINDING SITE FOR RESIDUE ZN B 400 source : AC1 4) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 5) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 6) chain A residue 94 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 7) chain A residue 75 type sequence E description BINDING SITE FOR RESIDUE CA B 402 source : AC3 8) chain B residue 328 type sequence E description BINDING SITE FOR RESIDUE CA B 402 source : AC3 9) chain B residue 350 type sequence Q description BINDING SITE FOR RESIDUE CA B 402 source : AC3 10) chain A residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA B 403 source : AC4 11) chain B residue 275 type sequence E description BINDING SITE FOR RESIDUE CA B 403 source : AC4 12) chain B residue 233 type sequence I description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 13) chain B residue 251 type sequence N description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 14) chain B residue 262 type sequence H description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 15) chain B residue 263 type sequence G description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 16) chain B residue 264 type sequence E description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 17) chain B residue 290 type sequence P description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 18) chain B residue 291 type sequence C description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 19) chain B residue 294 type sequence C description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 20) chain B residue 355 type sequence D description BINDING SITE FOR RESIDUE HPY B 410 source : AC5 21) chain A residue 33 type sequence I description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 22) chain A residue 51 type sequence N description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 23) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 24) chain A residue 63 type sequence G description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 25) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 26) chain A residue 90 type sequence P description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 27) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 28) chain A residue 94 type sequence C description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 29) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE HPY A 411 source : AC6 30) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE ACY A 420 source : AC7 31) chain B residue 273 type sequence R description BINDING SITE FOR RESIDUE ACY A 420 source : AC7 32) chain B residue 302 type sequence G description BINDING SITE FOR RESIDUE ACY B 421 source : AC8 33) chain B residue 326 type sequence G description BINDING SITE FOR RESIDUE ACY B 421 source : AC8 34) chain B residue 327 type sequence H description BINDING SITE FOR RESIDUE ACY B 421 source : AC8 35) chain B residue 353 type sequence F description BINDING SITE FOR RESIDUE ACY B 421 source : AC8 36) chain A residue 77 type sequence K description BINDING SITE FOR RESIDUE ACY B 422 source : AC9 37) chain B residue 240 type sequence N description BINDING SITE FOR RESIDUE ACY B 422 source : AC9 38) chain B residue 281 type sequence D description BINDING SITE FOR RESIDUE ACY B 422 source : AC9 39) chain B residue 304 type sequence P description BINDING SITE FOR RESIDUE ACY B 422 source : AC9 40) chain B residue 353 type sequence F description BINDING SITE FOR RESIDUE ACY B 422 source : AC9 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) 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 51) 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 52) 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 53) chain A residue 91 type catalytic sequence C description 636 source MCSA : MCSA1 54) chain A residue 62 type catalytic sequence H description 636 source MCSA : MCSA1 55) chain A residue 64 type catalytic sequence E description 636 source MCSA : MCSA1 56) chain A residue 89 type catalytic sequence S description 636 source MCSA : MCSA1 57) chain A residue 94 type catalytic sequence C description 636 source MCSA : MCSA1 58) chain B residue 291 type catalytic sequence C description 636 source MCSA : MCSA2 59) chain B residue 262 type catalytic sequence H description 636 source MCSA : MCSA2 60) chain B residue 264 type catalytic sequence E description 636 source MCSA : MCSA2 61) chain B residue 289 type catalytic sequence S description 636 source MCSA : MCSA2 62) chain B residue 294 type catalytic sequence C description 636 source MCSA : MCSA2 63) 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

Display surface Download Links