eF-site ID 5aiu-ABCEF PDB Code 5aiu Chain A, B, C, E, F click to enlarge Title A complex of RNF4-RING domain, Ubc13-Ub (isopeptide crosslink) Classification LIGASE/SIGNALING PROTEIN Compound E3 UBIQUITIN-PROTEIN LIGASE RNF4 Source (UBC_HUMAN) Sequence A:  SGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDS LKNANTCPTCRKKINRYHPIYIGSGTVSCPICMDGYSEIV QNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKIYHP IYI B:  AGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAG PQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVD KLGRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDDPL ANDVAEQWKTNEAQAIETARAWTRLYAMNN C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E:  AGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAG PQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVD KLGRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDDPL ANDVAEQWKTNEAQAIETARAWTRLYAMNN F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 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 Functional site 1) chain A residue 136 type sequence C description BINDING SITE FOR RESIDUE ZN A 800 source : AC1 2) chain A residue 139 type sequence C description BINDING SITE FOR RESIDUE ZN A 800 source : AC1 3) chain A residue 163 type sequence C description BINDING SITE FOR RESIDUE ZN A 800 source : AC1 4) chain A residue 166 type sequence C description BINDING SITE FOR RESIDUE ZN A 800 source : AC1 5) chain A residue 158 type sequence C description BINDING SITE FOR RESIDUE ZN A 801 source : AC2 6) chain A residue 160 type sequence H description BINDING SITE FOR RESIDUE ZN A 801 source : AC2 7) chain A residue 177 type sequence C description BINDING SITE FOR RESIDUE ZN A 801 source : AC2 8) chain A residue 180 type sequence C description BINDING SITE FOR RESIDUE ZN A 801 source : AC2 9) chain A residue 201 type sequence C description BINDING SITE FOR RESIDUE ZN A 802 source : AC3 10) chain A residue 204 type sequence C description BINDING SITE FOR RESIDUE ZN A 802 source : AC3 11) chain A residue 228 type sequence C description BINDING SITE FOR RESIDUE ZN A 802 source : AC3 12) chain A residue 231 type sequence C description BINDING SITE FOR RESIDUE ZN A 802 source : AC3 13) chain A residue 223 type sequence C description BINDING SITE FOR RESIDUE ZN A 803 source : AC4 14) chain A residue 225 type sequence H description BINDING SITE FOR RESIDUE ZN A 803 source : AC4 15) chain A residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN A 803 source : AC4 16) chain A residue 245 type sequence C description BINDING SITE FOR RESIDUE ZN A 803 source : AC4 17) chain E residue 47 type sequence F description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 18) chain E residue 52 type sequence F description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 19) chain E residue 74 type sequence K description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 20) chain E residue 75 type sequence I description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 21) chain E residue 76 type sequence Y description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 22) chain E residue 140 type sequence A description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 23) chain E residue 143 type sequence W description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 24) chain E residue 144 type sequence T description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 25) chain E residue 147 type sequence Y description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 26) chain E residue 148 type sequence A description BINDING SITE FOR RESIDUE EDO E 1152 source : AC5 27) chain F residue 45 type sequence F description BINDING SITE FOR RESIDUE EDO F 1077 source : AC6 28) chain F residue 46 type sequence A description BINDING SITE FOR RESIDUE EDO F 1077 source : AC6 29) chain F residue 47 type sequence G description BINDING SITE FOR RESIDUE EDO F 1077 source : AC6 30) chain F residue 68 type sequence H description BINDING SITE FOR RESIDUE EDO F 1077 source : AC6 31) chain B residue 47 type sequence F description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 32) chain B residue 52 type sequence F description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 33) chain B residue 74 type sequence K description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 34) chain B residue 75 type sequence I description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 35) chain B residue 76 type sequence Y description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 36) chain B residue 140 type sequence A description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 37) chain B residue 143 type sequence W description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 38) chain B residue 144 type sequence T description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 39) chain B residue 147 type sequence Y description BINDING SITE FOR RESIDUE EDO B 1152 source : AC7 40) chain B residue 106 type sequence L description BINDING SITE FOR RESIDUE EDO C 1077 source : AC8 41) chain C residue 45 type sequence F description BINDING SITE FOR RESIDUE EDO C 1077 source : AC8 42) chain C residue 46 type sequence A description BINDING SITE FOR RESIDUE EDO C 1077 source : AC8 43) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE EDO C 1077 source : AC8 44) chain C residue 68 type sequence H description BINDING SITE FOR RESIDUE EDO C 1077 source : AC8 45) chain A residue 193 type sequence Y description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 46) chain A residue 202 type sequence P description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 47) chain A residue 225 type sequence H description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 48) chain A residue 226 type sequence V description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 49) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 50) chain A residue 244 type sequence T description BINDING SITE FOR RESIDUE EDO A 1260 source : AC9 51) chain B residue 15 type sequence L description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 52) chain B residue 19 type sequence P description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 53) chain B residue 20 type sequence V description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 54) chain B residue 23 type sequence I description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 55) chain B residue 24 type sequence K description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 56) chain B residue 25 type sequence A description BINDING SITE FOR RESIDUE EDO B 1153 source : BC1 57) chain C residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 58) chain F residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 59) chain C residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 60) chain F residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) chain E residue 92 type MOD_RES sequence A 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 72) chain C residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 73) chain C residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 74) chain F residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 75) chain F residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 76) chain C residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 77) chain F residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 78) chain A residue 158 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 79) chain A residue 160 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 80) chain A residue 163 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 81) chain A residue 166 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 82) chain A residue 177 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 83) chain A residue 180 type SITE sequence C description Essential for function source Swiss-Prot : SWS_FT_FI2 84) chain A residue 158-167 type prosite sequence CGHVFCSQCL description ZF_RING_1 Zinc finger RING-type signature. CgHvFCsqCL source prosite : PS00518 85) chain A residue 223-232 type prosite sequence CGHVFCSQCL description ZF_RING_1 Zinc finger RING-type signature. CgHvFCsqCL source prosite : PS00518 86) chain C residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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

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