eF-site ID 2fif-ABCDEF PDB Code 2fif Chain A, B, C, D, E, F click to enlarge Title Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin Classification PROTEIN TURNOVER/ENDOCYTOSIS Compound Ubiquitin Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL B:  SELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQED WELAERLQREEEEAFASSQ C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL D:  ELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDW ELAERLQREEEEAFASSQ E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRL F:  LLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWE LAERLQREEEEAFASS Description Functional site 1) chain B residue 19 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 2) chain B residue 23 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 3) chain B residue 35 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 4) chain B residue 38 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 5) chain D residue 19 type sequence C description BINDING SITE FOR RESIDUE ZN D 902 source : AC2 6) chain D residue 23 type sequence C description BINDING SITE FOR RESIDUE ZN D 902 source : AC2 7) chain D residue 35 type sequence C description BINDING SITE FOR RESIDUE ZN D 902 source : AC2 8) chain D residue 38 type sequence C description BINDING SITE FOR RESIDUE ZN D 902 source : AC2 9) chain F residue 19 type sequence C description BINDING SITE FOR RESIDUE ZN F 903 source : AC3 10) chain F residue 23 type sequence C description BINDING SITE FOR RESIDUE ZN F 903 source : AC3 11) chain F residue 35 type sequence C description BINDING SITE FOR RESIDUE ZN F 903 source : AC3 12) chain F residue 38 type sequence C description BINDING SITE FOR RESIDUE ZN F 903 source : AC3 13) chain A residue 42 type sequence R description BINDING SITE FOR RESIDUE SO4 A 101 source : AC4 14) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE SO4 A 101 source : AC4 15) chain C residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 A 101 source : AC4 16) chain C residue 34 type sequence E description BINDING SITE FOR RESIDUE SO4 A 101 source : AC4 17) chain A residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 18) chain C residue 72 type ZN_FING sequence R description A20-type => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 19) chain E residue 54 type ZN_FING sequence R description A20-type => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 20) chain E residue 72 type ZN_FING sequence R description A20-type => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 19 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 23 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 23) chain F residue 35 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 24) chain F residue 38 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 23 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 35 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 38 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 19 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 29) chain D residue 23 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 30) chain D residue 35 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 38 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 32) chain F residue 19 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 34) chain C residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 35) chain E residue 65 type MOD_RES sequence S description Phosphoserine; by PINK1 => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 37) chain C residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 38) chain C residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 40) chain C residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 42) chain E residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 43) chain E residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 44) chain E residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 45) chain E residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 46) chain E residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 48) chain E residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 49) chain E residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 27 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 51) chain A residue 29 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 52) chain A residue 33 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 53) chain A residue 48 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 54) chain A residue 63 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 55) chain C residue 6 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5 56) chain C residue 11 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48 source Swiss-Prot : SWS_FT_FI5

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