eF-site ID 6j6t-ABCD PDB Code 6j6t Chain A, B, C, D click to enlarge Title Crystal Structure of HDA15 HD domain Classification GENE REGULATION Compound Histone deacetylase 15 Source (HDA15_ARATH) Sequence A:  SSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLAT AGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLL YSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNG FALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKV LIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGT GAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLP IASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQM LGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGELPIA TTPSVAGLQTVLDVLNIQLEFWPSLAISYSKLL B:  ATSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASL ATAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQ LLYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVK NGFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAK KVLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYP GTGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVV LPIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMT QMLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGEAT TPSVAGLQTVLDVLNIQLEFWPSLAISYSKLLSELE C:  TAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLATAG VFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLLYS YFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNGFA LVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKVLI VDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGTGA ADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLPIA SAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQMLG DLCGGKMLVILEGGYNLRSISASATAVIKVLLGESVAGLQ TVLDVLNIQLEFWPSLAISYSKLL D:  TSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLA TAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQL LYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKN GFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKK VLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPG TGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVL PIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQ MLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGETPS VAGLQTVLDVLNIQLEFWPSLAISYSKLLSE Description Functional site 1) chain A residue 313 type sequence D description binding site for residue ZN A 601 source : AC1 2) chain A residue 315 type sequence H description binding site for residue ZN A 601 source : AC1 3) chain A residue 404 type sequence D description binding site for residue ZN A 601 source : AC1 4) chain A residue 311 type sequence D description binding site for residue K A 602 source : AC2 5) chain A residue 313 type sequence D description binding site for residue K A 602 source : AC2 6) chain A residue 315 type sequence H description binding site for residue K A 602 source : AC2 7) chain A residue 334 type sequence S description binding site for residue K A 602 source : AC2 8) chain A residue 335 type sequence L description binding site for residue K A 602 source : AC2 9) chain A residue 204 type sequence T description binding site for residue SO4 A 603 source : AC3 10) chain A residue 205 type sequence K description binding site for residue SO4 A 603 source : AC3 11) chain A residue 206 type sequence Q description binding site for residue SO4 A 603 source : AC3 12) chain C residue 213 type sequence T description binding site for residue SO4 A 603 source : AC3 13) chain C residue 214 type sequence S description binding site for residue SO4 A 603 source : AC3 14) chain C residue 215 type sequence E description binding site for residue SO4 A 603 source : AC3 15) chain A residue 213 type sequence T description binding site for residue SO4 A 604 source : AC4 16) chain A residue 214 type sequence S description binding site for residue SO4 A 604 source : AC4 17) chain A residue 215 type sequence E description binding site for residue SO4 A 604 source : AC4 18) chain B residue 313 type sequence D description binding site for residue ZN B 601 source : AC5 19) chain B residue 315 type sequence H description binding site for residue ZN B 601 source : AC5 20) chain B residue 404 type sequence D description binding site for residue ZN B 601 source : AC5 21) chain B residue 311 type sequence D description binding site for residue K B 602 source : AC6 22) chain B residue 313 type sequence D description binding site for residue K B 602 source : AC6 23) chain B residue 315 type sequence H description binding site for residue K B 602 source : AC6 24) chain B residue 334 type sequence S description binding site for residue K B 602 source : AC6 25) chain B residue 335 type sequence L description binding site for residue K B 602 source : AC6 26) chain B residue 327 type sequence N description binding site for residue SO4 B 603 source : AC7 27) chain B residue 328 type sequence K description binding site for residue SO4 B 603 source : AC7 28) chain B residue 329 type sequence S description binding site for residue SO4 B 603 source : AC7 29) chain B residue 445 type sequence N description binding site for residue SO4 B 604 source : AC8 30) chain B residue 447 type sequence R description binding site for residue SO4 B 604 source : AC8 31) chain D residue 148 type sequence S description binding site for residue SO4 B 604 source : AC8 32) chain D residue 265 type sequence K description binding site for residue SO4 B 604 source : AC8 33) chain A residue 157 type sequence R description binding site for residue SO4 B 605 source : AC9 34) chain A residue 243 type sequence R description binding site for residue SO4 B 605 source : AC9 35) chain B residue 204 type sequence T description binding site for residue SO4 B 605 source : AC9 36) chain B residue 205 type sequence K description binding site for residue SO4 B 605 source : AC9 37) chain B residue 246 type sequence R description binding site for residue SO4 B 605 source : AC9 38) chain C residue 313 type sequence D description binding site for residue ZN C 601 source : AD1 39) chain C residue 315 type sequence H description binding site for residue ZN C 601 source : AD1 40) chain C residue 404 type sequence D description binding site for residue ZN C 601 source : AD1 41) chain C residue 311 type sequence D description binding site for residue K C 602 source : AD2 42) chain C residue 313 type sequence D description binding site for residue K C 602 source : AD2 43) chain C residue 315 type sequence H description binding site for residue K C 602 source : AD2 44) chain C residue 334 type sequence S description binding site for residue K C 602 source : AD2 45) chain C residue 335 type sequence L description binding site for residue K C 602 source : AD2 46) chain C residue 179 type sequence R description binding site for residue SO4 C 603 source : AD3 47) chain D residue 313 type sequence D description binding site for residue ZN D 601 source : AD4 48) chain D residue 315 type sequence H description binding site for residue ZN D 601 source : AD4 49) chain D residue 404 type sequence D description binding site for residue ZN D 601 source : AD4 50) chain D residue 311 type sequence D description binding site for residue K D 602 source : AD5 51) chain D residue 313 type sequence D description binding site for residue K D 602 source : AD5 52) chain D residue 315 type sequence H description binding site for residue K D 602 source : AD5 53) chain D residue 334 type sequence S description binding site for residue K D 602 source : AD5 54) chain D residue 335 type sequence L description binding site for residue K D 602 source : AD5 55) chain D residue 179 type sequence R description binding site for residue SO4 D 603 source : AD6 56) chain D residue 204 type sequence T description binding site for residue SO4 D 604 source : AD7 57) chain D residue 205 type sequence K description binding site for residue SO4 D 604 source : AD7 58) chain A residue 277 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000305|PubMed:31061103 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 277 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000305|PubMed:31061103 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 277 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000305|PubMed:31061103 source Swiss-Prot : SWS_FT_FI1 61) chain D residue 277 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000305|PubMed:31061103 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 63) chain D residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 64) chain D residue 315 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 65) chain D residue 404 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 66) chain A residue 315 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 67) chain A residue 404 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 68) chain B residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 69) chain B residue 315 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 70) chain B residue 404 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 71) chain C residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 72) chain C residue 315 type BINDING sequence H description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 73) chain C residue 404 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI2 74) chain A residue 444 type SITE sequence Y description Polarizes the scissile carbonyl of the substrate => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI3 75) chain B residue 444 type SITE sequence Y description Polarizes the scissile carbonyl of the substrate => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI3 76) chain C residue 444 type SITE sequence Y description Polarizes the scissile carbonyl of the substrate => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI3 77) chain D residue 444 type SITE sequence Y description Polarizes the scissile carbonyl of the substrate => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T source Swiss-Prot : SWS_FT_FI3

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