eF-site ID 5ait-ABCDEFG PDB Code 5ait Chain A, B, C, D, E, F, G click to enlarge Title A complex of of RNF4-RING domain, UbeV2, Ubc13-Ub (isopeptide crosslink) Classification LIGASE/SIGNALING PROTEIN Compound E3 UBIQUITIN-PROTEIN LIGASE RNF4 Source (UB2V2_HUMAN) Sequence A:  SGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDS LKNANTCPTCRKKINHKRYHPIYIGSGTVSCPICMDGYSE IVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKIN HKRYHPIYI B:  LPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQ DSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKL GRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDDPLAN DVAEQWKTNEAQAIETARAWTRLYAMN C:  QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ RLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG D:  GVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTR WTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTK INMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRL MMSKENMKLPQPPEGQTYNN E:  LPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQ DSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKL GRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDDPLAN DVAEQWKTNEAQAIETARAWTRLYAMN F:  QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ RLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG G:  GVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTR WTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTK INMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRL MMSKENMKLPQPPEGQTY Description (1)  E3 UBIQUITIN-PROTEIN LIGASE RNF4 (E.C.6.3.2.-), UBIQUITIN-CONJUGATING ENZYME E2 N (E.C.6.3.2.19), POLYUBIQUITIN-C, UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2 Functional site 1) chain A residue 136 type sequence C description BINDING SITE FOR RESIDUE ZN A 1260 source : AC1 2) chain A residue 139 type sequence C description BINDING SITE FOR RESIDUE ZN A 1260 source : AC1 3) chain A residue 151 type sequence R description BINDING SITE FOR RESIDUE ZN A 1260 source : AC1 4) chain A residue 163 type sequence C description BINDING SITE FOR RESIDUE ZN A 1260 source : AC1 5) chain A residue 166 type sequence C description BINDING SITE FOR RESIDUE ZN A 1260 source : AC1 6) chain A residue 158 type sequence C description BINDING SITE FOR RESIDUE ZN A 1261 source : AC2 7) chain A residue 160 type sequence H description BINDING SITE FOR RESIDUE ZN A 1261 source : AC2 8) chain A residue 177 type sequence C description BINDING SITE FOR RESIDUE ZN A 1261 source : AC2 9) chain A residue 180 type sequence C description BINDING SITE FOR RESIDUE ZN A 1261 source : AC2 10) chain A residue 201 type sequence C description BINDING SITE FOR RESIDUE ZN A 1262 source : AC3 11) chain A residue 204 type sequence C description BINDING SITE FOR RESIDUE ZN A 1262 source : AC3 12) chain A residue 228 type sequence C description BINDING SITE FOR RESIDUE ZN A 1262 source : AC3 13) chain A residue 231 type sequence C description BINDING SITE FOR RESIDUE ZN A 1262 source : AC3 14) chain A residue 223 type sequence C description BINDING SITE FOR RESIDUE ZN A 1263 source : AC4 15) chain A residue 225 type sequence H description BINDING SITE FOR RESIDUE ZN A 1263 source : AC4 16) chain A residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN A 1263 source : AC4 17) chain A residue 245 type sequence C description BINDING SITE FOR RESIDUE ZN A 1263 source : AC4 18) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 19) chain E residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 223 type MOD_RES sequence C description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 225 type MOD_RES sequence H description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 228 type MOD_RES sequence C description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 231 type MOD_RES sequence C description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 242 type MOD_RES sequence C description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 245 type MOD_RES sequence C description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 158-167 type prosite sequence CGHVFCSQCL description ZF_RING_1 Zinc finger RING-type signature. CgHvFCsqCL source prosite : PS00518 27) chain A residue 223-232 type prosite sequence CGHVFCSQCL description ZF_RING_1 Zinc finger RING-type signature. CgHvFCsqCL source prosite : PS00518 28) chain C residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 29) chain B residue 92 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000269|PubMed:16112642, ECO:0000269|PubMed:16122702 source Swiss-Prot : SWS_FT_FI3 30) chain E residue 92 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000269|PubMed:16112642, ECO:0000269|PubMed:16122702 source Swiss-Prot : SWS_FT_FI3

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