eF-site ID 4dnc-ABDE PDB Code 4dnc Chain A, B, D, E click to enlarge Title Crystal structure of human MOF in complex with MSL1 Classification TRANSCRIPTION Compound Histone acetyltransferase KAT8 Source Homo sapiens (Human) (MSL1_HUMAN) Sequence A:  YVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYM KYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHK IYCQNLCLLAKLFLDHXTLYFDVEPFVFYILTEVDRQGAH IVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSY ELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR GTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICV TPKLVEEHLKSAQYKKPPITVDSVCLKWAPPK B:  KYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY MKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDH KIYCQNLCLLAKLFLDHXTLYFDVEPFVFYILTEVDRQGA HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFS YELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF RGTLSIKDLSQMTSITQNDIISTLQSLNMVKYQHVICVTP KLVEEHLKSAQYKKPPITVDSVCLKWAP D:  LAVPSWRDHSVEPLRDPLENLDDSVFSKRHAKLELDEKRR KR E:  LAVPSWRDHSVEPLDPNPSLLENLDDSVFSKRHAKLELDE KRRKRW Description (1)  Histone acetyltransferase KAT8 (E.C.2.3.1.48), Male-specific lethal 1 homolog Functional site 1) chain A residue 210 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 2) chain A residue 213 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 3) chain A residue 226 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 4) chain A residue 230 type sequence C description BINDING SITE FOR RESIDUE ZN A 501 source : AC1 5) chain B residue 210 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC2 6) chain B residue 213 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC2 7) chain B residue 226 type sequence H description BINDING SITE FOR RESIDUE ZN B 501 source : AC2 8) chain B residue 230 type sequence C description BINDING SITE FOR RESIDUE ZN B 501 source : AC2 9) chain A residue 207-232 type ZN_FING sequence LWLCEYCLKYMKYEKSYRFHLGQCQW description C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126 source Swiss-Prot : SWS_FT_FI1 10) chain B residue 207-232 type ZN_FING sequence LWLCEYCLKYMKYEKSYRFHLGQCQW description C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 350 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 12) chain B residue 350 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 13) chain A residue 317 type BINDING sequence I description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 324 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 432 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 324 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 354 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 363 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 354 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 363 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 432 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 317 type BINDING sequence I description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 274 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 24) chain B residue 274 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 25) chain A residue 348 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 348 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5

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