eF-site ID 1q17-A PDB Code 1q17 Chain A click to enlarge Title Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide Classification HYDROLASE Compound HST2 protein Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (HST2_YEAST) Sequence A:  GMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAGIS TSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQSDP LPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYTQN IDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQVFK SKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSETW LNDSEWLREKIQPLVIVVGTSLAVYPFASLPEEIPRKVKR VLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEELGWQ EDFEKILTAQ Description Functional site 1) chain A residue 143 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 2) chain A residue 146 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 3) chain A residue 170 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 4) chain A residue 173 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 5) chain A residue 204 type sequence R description BINDING SITE FOR RESIDUE CL A 703 source : AC6 6) chain A residue 240 type sequence R description BINDING SITE FOR RESIDUE CL A 703 source : AC6 7) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 8) chain A residue 33 type sequence A description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 9) chain A residue 34 type sequence G description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 10) chain A residue 37 type sequence T description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 11) chain A residue 43 type sequence D description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 12) chain A residue 44 type sequence F description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 13) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 14) chain A residue 52 type sequence Y description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 15) chain A residue 115 type sequence Q description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 16) chain A residue 135 type sequence H description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 17) chain A residue 223 type sequence G description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 18) chain A residue 224 type sequence T description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 19) chain A residue 225 type sequence S description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 20) chain A residue 228 type sequence V description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 21) chain A residue 248 type sequence N description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 22) chain A residue 249 type sequence L description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 23) chain A residue 250 type sequence E description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 24) chain A residue 268 type sequence Q description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 25) chain A residue 269 type sequence Y description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 26) chain A residue 270 type sequence S description BINDING SITE FOR RESIDUE APR A 1001 source : AC8 27) chain A residue 42 type catalytic sequence P description 240 source MCSA : MCSA1 28) chain A residue 43 type catalytic sequence D description 240 source MCSA : MCSA1 29) chain A residue 44 type catalytic sequence F description 240 source MCSA : MCSA1 30) chain A residue 45 type catalytic sequence R description 240 source MCSA : MCSA1 31) chain A residue 116 type catalytic sequence N description 240 source MCSA : MCSA1 32) chain A residue 118 type catalytic sequence D description 240 source MCSA : MCSA1 33) chain A residue 135 type catalytic sequence H description 240 source MCSA : MCSA1 34) chain A residue 143 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 146 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 170 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 173 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 135 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 115 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 223 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 248 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 270 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI4

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