eF-site ID 2giv-A PDB Code 2giv Chain A click to enlarge Title Human MYST histone acetyltransferase 1 Classification TRANSFERASE Compound Probable histone acetyltransferase MYST1 Source (NP_115564) Sequence A:  KYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY MKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVHEVDGKDH KIYCQNLCLLAKLFLDHXTLYFDVEPFVFYILTEVDRQGA HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFS YELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLENLRSI KDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLV EEHLPPITVDSVCLKWAP Description Functional site 1) chain A residue 37 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 2) chain A residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 3) chain A residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 4) chain A residue 57 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 5) chain A residue 17 type sequence D description BINDING SITE FOR RESIDUE CL A 502 source : AC2 6) chain A residue 19 type sequence W description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 7) chain A residue 97 type sequence F description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 8) chain A residue 98 type sequence L description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 9) chain A residue 142 type sequence A description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 10) chain A residue 143 type sequence C description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 11) chain A residue 144 type sequence I description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 12) chain A residue 145 type sequence L description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 13) chain A residue 146 type sequence T description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 14) chain A residue 151 type sequence Q description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 15) chain A residue 152 type sequence R description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 16) chain A residue 153 type sequence R description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 17) chain A residue 154 type sequence G description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 18) chain A residue 156 type sequence G description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 19) chain A residue 157 type sequence K description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 20) chain A residue 177 type sequence E description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 21) chain A residue 180 type sequence L description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 22) chain A residue 181 type sequence S description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 23) chain A residue 183 type sequence L description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 24) chain A residue 186 type sequence L description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 25) chain A residue 187 type sequence S description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 26) chain A residue 190 type sequence S description BINDING SITE FOR RESIDUE ACO A 500 source : AC3 27) chain A residue 101 type MOD_RES sequence X description N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 175 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 144 type BINDING sequence I description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 151 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 181 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 190 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 34-59 type ZN_FING sequence LWLCEYCLKYMKYEKSYRFHLGQCQW description C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 177 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000303|PubMed:21217699, ECO:0000303|PubMed:22020126, ECO:0000305 source Swiss-Prot : SWS_FT_FI2

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