eF-site ID 4ljp-AB PDB Code 4ljp Chain A, B click to enlarge Title Structure of an active ligase (HOIP-H889A)/ubiquitin transfer complex Classification LIGASE Compound E3 ubiquitin-protein ligase RNF31 Source ORGANISM_COMMON: bovine,cow,domestic cattle,domestic cow; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  AQGLAMYLQENGIDCPKCKFSYALARGGCMHFACTQCRHQ FCSGCYNAFYAKNKCPEPNCRVKKSLHGHHPRDCLFYLRD WTALRLQKLLQDNNVMFNTEPPAGARAVPGGGCRVIEQKE VPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLD PATLYEVEELETATERYLHVRPQPLAGEDPPAYQARLLQK LTEEVPLGQSIPRRR B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG Description Functional site 1) chain A residue 871 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 2) chain A residue 874 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 3) chain A residue 890 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 4) chain A residue 893 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 5) chain A residue 898 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 6) chain A residue 901 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 7) chain A residue 926 type sequence H description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 8) chain A residue 930 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 9) chain A residue 911 type sequence C description BINDING SITE FOR RESIDUE ZN A 1103 source : AC3 10) chain A residue 916 type sequence C description BINDING SITE FOR RESIDUE ZN A 1103 source : AC3 11) chain A residue 923 type sequence H description BINDING SITE FOR RESIDUE ZN A 1103 source : AC3 12) chain A residue 925 type sequence H description BINDING SITE FOR RESIDUE ZN A 1103 source : AC3 13) chain A residue 969 type sequence C description BINDING SITE FOR RESIDUE ZN A 1104 source : AC4 14) chain A residue 986 type sequence C description BINDING SITE FOR RESIDUE ZN A 1104 source : AC4 15) chain A residue 998 type sequence C description BINDING SITE FOR RESIDUE ZN A 1104 source : AC4 16) chain A residue 1001 type sequence H description BINDING SITE FOR RESIDUE ZN A 1104 source : AC4 17) chain B residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI6 18) chain B residue 54 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 19) chain B residue 72 type SITE sequence R description Interacts with activating enzyme source Swiss-Prot : SWS_FT_FI1 20) chain B residue 68 type SITE sequence H description Essential for function source Swiss-Prot : SWS_FT_FI2 21) chain B residue 76 type MOD_RES sequence G description ADP-ribosylglycine => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 874 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 890 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 893 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 898 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 901 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 916 type MOD_RES sequence C description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 925 type MOD_RES sequence H description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P62987 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 893-902 type prosite sequence CRHQFCSGCY description ZF_RING_1 Zinc finger RING-type signature. CrHqFCsgCY source prosite : PS00518 38) chain B residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299

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