eF-site ID 2yho-ABCDEFGH PDB Code 2yho Chain A, B, C, D, E, F, G, H click to enlarge Title The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor Classification LIGASE Compound E3 UBIQUITIN-PROTEIN LIGASE MYLIP Source Homo sapiens (Human) (UB2D1_HUMAN) Sequence A:  RVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESC AAQLQSCPVCRSRVEHVQHVYLPTHTS B:  GAMALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIM GPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNI NSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDP LVPDIAQIYKSDKEKYNRHAREWTQKYAM C:  RVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESC AAQLQSCPVCRSRVEHVQHVYLPTHTS D:  GAMALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIM GPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNI NSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDP LVPDIAQIYKSDKEKYNRHAREWTQKYAM E:  RVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESC AAQLQSCPVCRSRVEHVQHVYLPTHTSLLN F:  GAMALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIM GPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNI NSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDP LVPDIAQIYKSDKEKYNRHAREWTQKYAM G:  RVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESC AAQLQSCPVCRSRVEHVQHVYLPTHTSLLN H:  MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGP PDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINS NGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLV PDIAQIYKSDKEKYNRHAREWTQKYAM Description Functional site 1) chain A residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 2) chain A residue 390 type sequence C description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 3) chain A residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 4) chain A residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN A 1001 source : AC1 5) chain A residue 402 type sequence C description BINDING SITE FOR RESIDUE ZN A 1002 source : AC2 6) chain A residue 404 type sequence H description BINDING SITE FOR RESIDUE ZN A 1002 source : AC2 7) chain A residue 418 type sequence C description BINDING SITE FOR RESIDUE ZN A 1002 source : AC2 8) chain A residue 421 type sequence C description BINDING SITE FOR RESIDUE ZN A 1002 source : AC2 9) chain C residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN C 1001 source : AC3 10) chain C residue 390 type sequence C description BINDING SITE FOR RESIDUE ZN C 1001 source : AC3 11) chain C residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN C 1001 source : AC3 12) chain C residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN C 1001 source : AC3 13) chain F residue -1 type sequence G description BINDING SITE FOR RESIDUE ZN C 1001 source : AC3 14) chain C residue 402 type sequence C description BINDING SITE FOR RESIDUE ZN C 1002 source : AC4 15) chain C residue 404 type sequence H description BINDING SITE FOR RESIDUE ZN C 1002 source : AC4 16) chain C residue 418 type sequence C description BINDING SITE FOR RESIDUE ZN C 1002 source : AC4 17) chain C residue 421 type sequence C description BINDING SITE FOR RESIDUE ZN C 1002 source : AC4 18) chain E residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN E 1001 source : AC5 19) chain E residue 390 type sequence C description BINDING SITE FOR RESIDUE ZN E 1001 source : AC5 20) chain E residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN E 1001 source : AC5 21) chain E residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN E 1001 source : AC5 22) chain E residue 402 type sequence C description BINDING SITE FOR RESIDUE ZN E 1002 source : AC6 23) chain E residue 404 type sequence H description BINDING SITE FOR RESIDUE ZN E 1002 source : AC6 24) chain E residue 418 type sequence C description BINDING SITE FOR RESIDUE ZN E 1002 source : AC6 25) chain E residue 421 type sequence C description BINDING SITE FOR RESIDUE ZN E 1002 source : AC6 26) chain G residue 387 type sequence C description BINDING SITE FOR RESIDUE ZN G 1001 source : AC7 27) chain G residue 390 type sequence C description BINDING SITE FOR RESIDUE ZN G 1001 source : AC7 28) chain G residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN G 1001 source : AC7 29) chain G residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN G 1001 source : AC7 30) chain G residue 402 type sequence C description BINDING SITE FOR RESIDUE ZN G 1002 source : AC8 31) chain G residue 404 type sequence H description BINDING SITE FOR RESIDUE ZN G 1002 source : AC8 32) chain G residue 418 type sequence C description BINDING SITE FOR RESIDUE ZN G 1002 source : AC8 33) chain G residue 421 type sequence C description BINDING SITE FOR RESIDUE ZN G 1002 source : AC8 34) chain H residue 67 type sequence I description BINDING SITE FOR RESIDUE ACT H 1148 source : AC9 35) chain H residue 84 type sequence I description BINDING SITE FOR RESIDUE ACT H 1148 source : AC9 36) chain G residue 383 type sequence E description BINDING SITE FOR RESIDUE ACT G 1442 source : BC1 37) chain G residue 384 type sequence A description BINDING SITE FOR RESIDUE ACT G 1442 source : BC1 38) chain G residue 386 type sequence L description BINDING SITE FOR RESIDUE ACT G 1442 source : BC1 39) chain G residue 388 type sequence M description BINDING SITE FOR RESIDUE ACT G 1442 source : BC1 40) chain H residue 5 type sequence R description BINDING SITE FOR RESIDUE ACT H 1149 source : BC2 41) chain H residue 8 type sequence K description BINDING SITE FOR RESIDUE ACT H 1149 source : BC2 42) chain B residue 67 type sequence I description BINDING SITE FOR RESIDUE ACT B 1148 source : BC3 43) chain B residue 84 type sequence I description BINDING SITE FOR RESIDUE ACT B 1148 source : BC3 44) chain F residue 67 type sequence I description BINDING SITE FOR RESIDUE ACT F 1148 source : BC4 45) chain F residue 83 type sequence S description BINDING SITE FOR RESIDUE ACT F 1148 source : BC4 46) chain F residue 84 type sequence I description BINDING SITE FOR RESIDUE ACT F 1148 source : BC4 47) chain B residue 69 type sequence F description BINDING SITE FOR RESIDUE ACT B 1149 source : BC5 48) chain B residue 70 type sequence T description BINDING SITE FOR RESIDUE ACT B 1149 source : BC5 49) chain B residue 80 type sequence S description BINDING SITE FOR RESIDUE ACT B 1149 source : BC5 50) chain B residue 82 type sequence G description BINDING SITE FOR RESIDUE ACT B 1149 source : BC5 51) chain A residue 383 type sequence E description BINDING SITE FOR RESIDUE ACT A 1439 source : BC6 52) chain A residue 384 type sequence A description BINDING SITE FOR RESIDUE ACT A 1439 source : BC6 53) chain A residue 386 type sequence L description BINDING SITE FOR RESIDUE ACT A 1439 source : BC6 54) chain D residue 105 type sequence S description BINDING SITE FOR RESIDUE ACT H 1150 source : BC7 55) chain D residue 108 type sequence S description BINDING SITE FOR RESIDUE ACT H 1150 source : BC7 56) chain H residue 57 type sequence P description BINDING SITE FOR RESIDUE ACT H 1150 source : BC7 57) chain H residue 58 type sequence T description BINDING SITE FOR RESIDUE ACT H 1150 source : BC7 58) chain A residue 404 type sequence H description BINDING SITE FOR RESIDUE ACT A 1440 source : BC8 59) chain B residue 74-89 type prosite sequence YHPNINSNGSICLDIL description UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL source prosite : PS00183 60) chain B residue 85 type ACT_SITE sequence C description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 61) chain D residue 85 type ACT_SITE sequence C description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 62) chain F residue 85 type ACT_SITE sequence C description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 63) chain H residue 85 type ACT_SITE sequence C description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1

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