eF-site ID 2o3k-B PDB Code 2o3k Chain B click to enlarge Title Yeast Cytosine Deaminase D92E Triple Mutant bound to transition state analogue HPY Classification HYDROLASE Compound Cytosine deaminase Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FCY1_YEAST) Sequence B:  MASKWDQKGMDIAYEEALLGYKEGGVPIGGCLINNKDGSV LGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDTTLY TTLSPCEMCTGAIIMYGIPRCVIGENVNFKSKGEKYLQTR GHEVVVVDDERCKKLMKQFIDERPQDWFEDIGE 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 B residue 275 type sequence E description BINDING SITE FOR RESIDUE CA B 403 source : AC3 5) chain B residue 233 type sequence I description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 6) chain B residue 251 type sequence N description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 7) chain B residue 262 type sequence H description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 8) chain B residue 263 type sequence G description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 9) chain B residue 264 type sequence E description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 10) chain B residue 291 type sequence C description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 11) chain B residue 294 type sequence C description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 12) chain B residue 355 type sequence D description BINDING SITE FOR RESIDUE HPY B 410 source : AC4 13) 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 14) 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 15) 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 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 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 22) 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 23) 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

Display surface Download Links