eF-site ID 4lcd-ACE PDB Code 4lcd Chain A, C, E click to enlarge Title Structure of an Rsp5xUbxSna3 complex: Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3 Classification Ligase/protein binding Compound E3 ubiquitin-protein ligase RSP5 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (UBC_HUMAN) Sequence A:  VSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPS SLDQNVPQYKRDFRRKVIYFRSQPALRILPGQLHIKVRRK NIFEDAYQEIMRQTPEDLKKRLMIKFDGYGGVSREFFFLL SHEMFNPFYGLFEYSAYDNYTIQINPNSGINPEHLNYFKF IGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGV DAEVYNSLNWMLENSIDGVLDLTFSADDERFGEVVTVDLK PDGRNIEVTDGNKKEYVELYTQWRIVDRVQEQFKAFMDGF NELIPEDLVTVFDERELELLIGGIAEIDIEDWKKHTDYRG YQESDEVIQWFWKAVSEWDNEQRARLLQFTTGTSRIPVNG FKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYV DYDSMKQKLTLAVEETIGF C:  QPPAYDED E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRC Description Functional site 1) chain E residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 2) chain E residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 3) chain E 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 4) chain E residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 5) chain E 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_FI5 6) chain E 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_FI6 7) chain E 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_FI7 8) chain E 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_FI7 9) chain E 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_FI10 10) chain E residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 11) chain E residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 12) chain A residue 393-418 type prosite sequence WEMRLTNTARVYFVDHNTKTTTWDDP description WW_DOMAIN_1 WW/rsp5/WWP domain signature. Wemrltntarv.YFvdhntktTTWDDP source prosite : PS01159 13) chain E 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_FI9 14) chain E 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_FI8

Display surface Download Links