eF-site ID 4auq-ABCDEF PDB Code 4auq Chain A, B, C, D, E, F click to enlarge Title Structure of BIRC7-UbcH5b-Ub complex. Classification LIGASE/LIGASE/SIGNALLING PROTEIN Compound UBIQUITIN-CONJUGATING ENZYME E2 D2 Source (UBC_HUMAN) Sequence A:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPAINSN GSISLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM B:  QLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQL CPICRAPVRSRVRTFLS C:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG D:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPAINSN GSISLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM E:  QLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQL CPICRAPVRSRVRTFLS F:  QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ RLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG Description Functional site 1) chain B residue 252 type sequence C description BINDING SITE FOR RESIDUE ZN B 1299 source : AC1 2) chain B residue 255 type sequence C description BINDING SITE FOR RESIDUE ZN B 1299 source : AC1 3) chain B residue 272 type sequence C description BINDING SITE FOR RESIDUE ZN B 1299 source : AC1 4) chain B residue 275 type sequence C description BINDING SITE FOR RESIDUE ZN B 1299 source : AC1 5) chain B residue 267 type sequence C description BINDING SITE FOR RESIDUE ZN B 1300 source : AC2 6) chain B residue 269 type sequence H description BINDING SITE FOR RESIDUE ZN B 1300 source : AC2 7) chain B residue 282 type sequence C description BINDING SITE FOR RESIDUE ZN B 1300 source : AC2 8) chain B residue 285 type sequence C description BINDING SITE FOR RESIDUE ZN B 1300 source : AC2 9) chain E residue 252 type sequence C description BINDING SITE FOR RESIDUE ZN E 1299 source : AC3 10) chain E residue 255 type sequence C description BINDING SITE FOR RESIDUE ZN E 1299 source : AC3 11) chain E residue 272 type sequence C description BINDING SITE FOR RESIDUE ZN E 1299 source : AC3 12) chain E residue 275 type sequence C description BINDING SITE FOR RESIDUE ZN E 1299 source : AC3 13) chain E residue 267 type sequence C description BINDING SITE FOR RESIDUE ZN E 1300 source : AC4 14) chain E residue 269 type sequence H description BINDING SITE FOR RESIDUE ZN E 1300 source : AC4 15) chain E residue 282 type sequence C description BINDING SITE FOR RESIDUE ZN E 1300 source : AC4 16) chain E residue 285 type sequence C description BINDING SITE FOR RESIDUE ZN E 1300 source : AC4 17) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 18) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 19) chain C 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 20) chain F 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 21) chain C 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 22) chain F 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 23) chain C 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 24) chain F 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 25) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 26) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 27) chain F residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 28) chain F residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 29) chain B residue 267-276 type prosite sequence CGHLVCAECA description ZF_RING_1 Zinc finger RING-type signature. CgHlVCaeCA source prosite : PS00518 30) chain A residue 76-85 type prosite sequence PAINSNGSIS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINSNGSIS source prosite : PS00152 31) chain C residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 32) chain C 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 33) chain F 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 34) chain C 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 35) chain F 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 36) chain C 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 37) chain F 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 38) chain C residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 39) chain F residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 40) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 41) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 42) chain C residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 43) chain F residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 44) chain C 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 45) chain C 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 46) chain F 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 47) chain F 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

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