eF-site ID 3mhs-ABCDE PDB Code 3mhs Chain A, B, C, D, E click to enlarge Title Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to ubiquitin aldehyde Classification Hydrolase/transcription regulator/protein binding Compound Ubiquitin carboxyl-terminal hydrolase 8 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (SGF73_YEAST) Sequence A:  AMSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEK FLNTMKCGTCHEINSGATFMCLQCGFCGCWNHSHFLSHSK QIGHIFGINSNNGLLFCFKCEDYIGNIDLINDAILAKYWD DVCTKTMVPSMERRDGLSGLINMGSTCFMSSILQCLIHNP YFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALN TSTNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIIN QIHQSYVLDLPNNNKQCECIVHTVFEGSLESSIVCPGCQN NSKTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFNY HCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSNR KLDDFIEFPTYLNMKNYCSTKEKDKENGKVPDIIYELIGI VSHKGTVNEGHYIAFCKISGGQWFKFNDSMVSSISQEEVL KEQAYLLFYTIRQVN B:  TAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKD LTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQ IREFLEEIVDT C:  EETITIDSISNGILNNLLTTLIQDIVARETTQQQLLKTRY PDLRSYYFDPNGSLDINGLQKQQESSQYIHCENCGRDVSA NRLAAHLQRCLSR D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX E:  DAEIKGIKPKVIEEYSGPSNDSWKSLMSSAKDTPLQYDHM NRESLKKYFNPNAQLIEDPLDKPIQYRVCEKCGKPLALTA IVDHLE Description (1)  Ubiquitin carboxyl-terminal hydrolase 8 (E.C.3.1.2.15), Protein SUS1, SAGA-associated factor 11, SAGA-associated factor 73, ubiquitin Functional site 1) chain A residue 236 type sequence Q description BINDING SITE FOR RESIDUE EDO A 1295 source : AC1 2) chain A residue 240 type sequence E description BINDING SITE FOR RESIDUE EDO A 1295 source : AC1 3) chain D residue 74 type sequence R description BINDING SITE FOR RESIDUE EDO A 1295 source : AC1 4) chain A residue 367 type sequence H description BINDING SITE FOR RESIDUE GOL A 1487 source : AC2 5) chain A residue 369 type sequence L description BINDING SITE FOR RESIDUE GOL A 1487 source : AC2 6) chain A residue 371 type sequence G description BINDING SITE FOR RESIDUE GOL A 1487 source : AC2 7) chain D residue 35 type sequence G description BINDING SITE FOR RESIDUE GOL A 1487 source : AC2 8) chain A residue 4 type sequence C description BINDING SITE FOR RESIDUE ZN A 472 source : AC3 9) chain A residue 6 type sequence H description BINDING SITE FOR RESIDUE ZN A 472 source : AC3 10) chain A residue 96 type sequence C description BINDING SITE FOR RESIDUE ZN A 472 source : AC3 11) chain A residue 99 type sequence C description BINDING SITE FOR RESIDUE ZN A 472 source : AC3 12) chain A residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN A 473 source : AC4 13) chain A residue 49 type sequence C description BINDING SITE FOR RESIDUE ZN A 473 source : AC4 14) chain A residue 68 type sequence C description BINDING SITE FOR RESIDUE ZN A 473 source : AC4 15) chain A residue 73 type sequence H description BINDING SITE FOR RESIDUE ZN A 473 source : AC4 16) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN A 474 source : AC5 17) chain A residue 63 type sequence C description BINDING SITE FOR RESIDUE ZN A 474 source : AC5 18) chain A residue 77 type sequence H description BINDING SITE FOR RESIDUE ZN A 474 source : AC5 19) chain A residue 83 type sequence H description BINDING SITE FOR RESIDUE ZN A 474 source : AC5 20) chain A residue 170 type sequence H description BINDING SITE FOR RESIDUE ZN A 475 source : AC6 21) chain A residue 174 type sequence C description BINDING SITE FOR RESIDUE ZN A 475 source : AC6 22) chain A residue 182 type sequence C description BINDING SITE FOR RESIDUE ZN A 475 source : AC6 23) chain A residue 185 type sequence C description BINDING SITE FOR RESIDUE ZN A 475 source : AC6 24) chain A residue 250 type sequence H description BINDING SITE FOR RESIDUE ZN A 476 source : AC7 25) chain A residue 271 type sequence C description BINDING SITE FOR RESIDUE ZN A 476 source : AC7 26) chain A residue 273 type sequence C description BINDING SITE FOR RESIDUE ZN A 476 source : AC7 27) chain A residue 276 type sequence H description BINDING SITE FOR RESIDUE ZN A 476 source : AC7 28) chain C residue 73 type sequence C description BINDING SITE FOR RESIDUE ZN C 100 source : AC8 29) chain C residue 76 type sequence C description BINDING SITE FOR RESIDUE ZN C 100 source : AC8 30) chain C residue 88 type sequence H description BINDING SITE FOR RESIDUE ZN C 100 source : AC8 31) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 100 source : AC8 32) chain E residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN E 97 source : AC9 33) chain E residue 93 type sequence H description BINDING SITE FOR RESIDUE ZN E 97 source : AC9 34) chain E residue 95 type sequence E description BINDING SITE FOR RESIDUE ZN E 97 source : AC9 35) chain A residue 289 type sequence C description BINDING SITE FOR RESIDUE ZN A 477 source : BC1 36) chain A residue 292 type sequence C description BINDING SITE FOR RESIDUE ZN A 477 source : BC1 37) chain A residue 336 type sequence C description BINDING SITE FOR RESIDUE ZN A 477 source : BC1 38) chain A residue 339 type sequence C description BINDING SITE FOR RESIDUE ZN A 477 source : BC1 39) chain D residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI6 40) chain D residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 source Swiss-Prot : SWS_FT_FI12 41) chain D residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 42) chain D residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 source Swiss-Prot : SWS_FT_FI8 43) chain D residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 source Swiss-Prot : SWS_FT_FI11 44) chain D residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 source Swiss-Prot : SWS_FT_FI9 45) chain D residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 46) chain A residue 138-153 type prosite sequence GLINMGSTCFMSSILQ description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLinmGStCFMSSiLQ source prosite : PS00972 47) chain A residue 411-428 type prosite sequence YELIGIVSHKGTVNEGHY description USP_2 Ubiquitin specific protease (USP) domain signature 2. YeLiGIvsHkGtvne..GHY source prosite : PS00973 48) chain D residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 source Swiss-Prot : SWS_FT_FI10 49) chain D residue 76 type MOD_RES sequence X description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 50) chain D residue 76 type CROSSLNK sequence X description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 51) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 52) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 53) chain D residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 source Swiss-Prot : SWS_FT_FI3 54) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 49 type MOD_RES sequence C description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 60 type MOD_RES sequence C description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 63 type MOD_RES sequence C description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 58) chain A residue 68 type MOD_RES sequence C description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 73 type MOD_RES sequence H description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 60) chain A residue 77 type MOD_RES sequence H description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 61) chain A residue 83 type MOD_RES sequence H description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 62) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2

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