eF-site ID 3b0a-ABDE PDB Code 3b0a Chain A, B, D, E click to enlarge Title Crystal structure of the mouse HOIL1-L-NZF in complex with linear di-ubiquitin Classification SIGNALING PROTEIN/METAL BINDING PROTEIN Compound Polyubiquitin-C Source Homo sapiens (Human) (HOIL1_MOUSE) Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRLRG B:  MPVGWQCPGCTFINKPTRPGCEMCCRARPETYQIPASYQP DEEERARLAGEEEALRQ D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIF VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E:  GPGHMPVGWQCPGCTFINKPTRPGCEMCCRARPETYQIPA SYQPDEEERARLAGEEEALRQYQ Description Functional site 1) chain A residue 118 type sequence R description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 2) chain A residue 125 type sequence Q description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 3) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 4) chain D residue 7 type sequence T description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 5) chain D residue 9 type sequence T description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 6) chain D residue 34 type sequence E description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 7) chain D residue 36 type sequence I description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 8) chain D residue 71 type sequence L description BINDING SITE FOR RESIDUE TAM A 153 source : AC1 9) chain B residue 197 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 10) chain B residue 200 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 11) chain B residue 211 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 12) chain B residue 214 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 13) chain E residue 197 type sequence C description BINDING SITE FOR RESIDUE ZN E 1 source : AC3 14) chain E residue 200 type sequence C description BINDING SITE FOR RESIDUE ZN E 1 source : AC3 15) chain E residue 211 type sequence C description BINDING SITE FOR RESIDUE ZN E 1 source : AC3 16) chain E residue 214 type sequence C description BINDING SITE FOR RESIDUE ZN E 1 source : AC3 17) chain A 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 18) chain D 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 19) chain A residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 20) chain A residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 21) chain D residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 22) chain D residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 23) chain A residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 24) chain D residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 25) chain A 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 26) chain D 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 27) chain A 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 28) chain D 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 29) chain A residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 30) chain D residue 66 type MOD_RES sequence T description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 32) chain D residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000269|PubMed:28525742 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 34) chain D residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI7 35) chain A 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 36) chain A 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 37) chain D 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 38) chain D 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 39) chain A 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 40) chain D 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 41) chain A 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 42) chain D 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 43) chain A 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 44) chain D 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 45) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 46) chain A residue 103-128 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 47) chain B residue 195-214 type prosite sequence WQCPGCTFINKPTRPGCEMC description ZF_RANBP2_1 Zinc finger RanBP2-type signature. WqCpg..CtfiNkptrpgCemC source prosite : PS01358

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