eF-site ID 1q17-B PDB Code 1q17 Chain B 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 null (HST2_YEAST) Sequence B:  HHGMASMSVSTASTEMSVRKIAAHMKSNPNAKVIFMVGAG ISTSCGIPDFRSPGTGLYHNLARLKLPYPEAVFDVDFFQS DPLPFYTLAKELYPGNFRPSKFHYLLKLFQDKDVLKRVYT QNIDTLERQAGVKDDLIIEAHGSFAHCHCIGCGKVYPPQV FKSKLAEHPIKDFVKCDVCGELVKPAIVFFGEDLPDSFSE TWLNDSEWLREKIPQQPLVIVVGTSLAVYPFASLPEEIPR KVKRVLCNLETVGDFKANKRPTDLIVHQYSDEFAEQLVEE LGWQEDFEKILTAQ Description Functional site 1) chain B residue 143 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC2 2) chain B residue 146 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC2 3) chain B residue 170 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC2 4) chain B residue 173 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC2 5) chain B residue 202 type sequence W description BINDING SITE FOR RESIDUE CL B 702 source : AC5 6) chain B residue 204 type sequence R description BINDING SITE FOR RESIDUE CL B 704 source : AC7 7) chain B residue 240 type sequence R description BINDING SITE FOR RESIDUE CL B 704 source : AC7 8) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 9) chain B residue 33 type sequence A description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 10) chain B residue 34 type sequence G description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 11) chain B residue 37 type sequence T description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 12) chain B residue 43 type sequence D description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 13) chain B residue 44 type sequence F description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 14) chain B residue 45 type sequence R description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 15) chain B residue 52 type sequence Y description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 16) chain B residue 115 type sequence Q description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 17) chain B residue 135 type sequence H description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 18) chain B residue 223 type sequence G description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 19) chain B residue 224 type sequence T description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 20) chain B residue 225 type sequence S description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 21) chain B residue 228 type sequence V description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 22) chain B residue 248 type sequence N description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 23) chain B residue 249 type sequence L description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 24) chain B residue 268 type sequence Q description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 25) chain B residue 269 type sequence Y description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 26) chain B residue 270 type sequence S description BINDING SITE FOR RESIDUE APR B 1002 source : AC9 27) chain B 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 28) chain B residue 270 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 115 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 223 type BINDING sequence G description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 248 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 source Swiss-Prot : SWS_FT_FI2 33) chain B 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 34) chain B 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 35) chain B 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 36) chain B 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 37) chain B residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 44 type catalytic sequence F description 240 source MCSA : MCSA2 39) chain B residue 42 type catalytic sequence P description 240 source MCSA : MCSA2 40) chain B residue 43 type catalytic sequence D description 240 source MCSA : MCSA2 41) chain B residue 45 type catalytic sequence R description 240 source MCSA : MCSA2 42) chain B residue 116 type catalytic sequence N description 240 source MCSA : MCSA2 43) chain B residue 118 type catalytic sequence D description 240 source MCSA : MCSA2 44) chain B residue 135 type catalytic sequence H description 240 source MCSA : MCSA2

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