eF-site ID 5l6h-C PDB Code 5l6h Chain C click to enlarge Title Uba1 in complex with Ub-ABPA3 covalent adduct Classification LIGASE Compound Ubiquitin-activating enzyme E1 1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (RS27A_YEAST) Sequence C:  AGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVE IAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQK RGDVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATD TVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDE FTVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGNF VRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYK KGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAA QLHLGFQALHQFAVRHNGELPRTMNDEDANELIKLVTDLS VQQPEVLGEGVDVNEDLIKELSYQARGDIPGVVAFFGGLV AQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTT QPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEML KNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDV GKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFND SFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLG TKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKID HTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSGD VKGVLESISDSLSSKPHNFEDCIKWARLEFEKKFNHDIKQ LLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHF VVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEF TPNANLKIQVNDDDPDDEIDQLVSSLPDPSTLAGFKLEPV DFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIA GRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFV NLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKL SDLIEHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERLN LPITQLVKLVTKKDIPAHVSTMILEIXADDKEGEDVEVPF ITIHL Description Functional site 1) chain C residue 21 type sequence R description binding site for residue SO4 C 1101 source : AD5 2) chain C residue 478 type sequence N description binding site for residue SO4 C 1101 source : AD5 3) chain C residue 481 type sequence R description binding site for residue SO4 C 1101 source : AD5 4) chain C residue 571 type sequence T description binding site for residue CL C 1102 source : AD6 5) chain C residue 514 type sequence N description binding site for residue CL C 1103 source : AD7 6) chain C residue 861 type sequence R description binding site for residue CL C 1104 source : AD8 7) chain C residue 1008 type sequence D description binding site for residue MG C 1106 source : AD9 8) chain C residue 713 type sequence R description binding site for residue GOL C 1107 source : AE1 9) chain C residue 714 type sequence A description binding site for residue GOL C 1107 source : AE1 10) chain C residue 846 type sequence F description binding site for residue GOL C 1107 source : AE1 11) chain C residue 267 type sequence K description binding site for residue GOL C 1108 source : AE2 12) chain C residue 271 type sequence Q description binding site for residue GOL C 1108 source : AE2 13) chain C residue 274 type sequence S description binding site for residue GOL C 1108 source : AE2 14) chain C residue 275 type sequence N description binding site for residue GOL C 1108 source : AE2 15) chain C residue 282 type sequence D description binding site for residue GOL C 1109 source : AE3 16) chain C residue 285 type sequence K description binding site for residue GOL C 1109 source : AE3 17) chain C residue 391 type sequence F description binding site for residue GOL C 1109 source : AE3 18) chain C residue 392 type sequence D description binding site for residue GOL C 1109 source : AE3 19) chain C residue 393 type sequence S description binding site for residue GOL C 1109 source : AE3 20) chain C residue 395 type sequence E description binding site for residue GOL C 1109 source : AE3 21) chain C residue 895 type sequence K description binding site for residue GOL C 1109 source : AE3 22) chain C residue 908 type sequence F description binding site for residue GOL C 1109 source : AE3 23) chain C residue 288 type sequence R description binding site for residue GOL C 1110 source : AE4 24) chain C residue 344 type sequence N description binding site for residue GOL C 1110 source : AE4 25) chain C residue 114 type sequence L description binding site for residue ACT C 1111 source : AE5 26) chain C residue 117 type sequence V description binding site for residue ACT C 1111 source : AE5 27) chain C residue 136 type sequence D description binding site for residue ACT C 1111 source : AE5 28) chain C residue 443 type sequence G description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 29) chain C residue 444 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 30) chain C residue 445 type sequence I description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 31) chain C residue 470 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 32) chain C residue 471 type sequence N description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 33) chain C residue 472 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 34) chain C residue 481 type sequence R description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 35) chain C residue 482 type sequence Q description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 36) chain C residue 494 type sequence K description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 37) chain C residue 520 type sequence V description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 38) chain C residue 542 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 39) chain C residue 543 type sequence L description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 40) chain C residue 544 type sequence D description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 41) chain C residue 545 type sequence N description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 42) chain C residue 548 type sequence A description binding site for Di-peptide 6O2 D 101 and GLY D 76 source : AE6 43) chain C residue 21 type catalytic sequence R description 307 source MCSA : MCSA3 44) chain C residue 481 type catalytic sequence R description 307 source MCSA : MCSA3 45) chain C residue 544 type catalytic sequence D description 307 source MCSA : MCSA3 46) chain C residue 600 type catalytic sequence C description 307 source MCSA : MCSA3 47) chain C residue 601 type catalytic sequence T description 307 source MCSA : MCSA3 48) chain C residue 603 type catalytic sequence R description 307 source MCSA : MCSA3 49) chain C residue 781 type catalytic sequence N description 307 source MCSA : MCSA3 50) chain C residue 782 type catalytic sequence D description 307 source MCSA : MCSA3 51) chain C residue 600 type catalytic sequence C description 939 source MCSA : MCSA4 52) chain C residue 601 type catalytic sequence T description 939 source MCSA : MCSA4 53) chain C residue 603 type catalytic sequence R description 939 source MCSA : MCSA4 54) chain C residue 781 type catalytic sequence N description 939 source MCSA : MCSA4 55) chain C residue 782 type catalytic sequence D description 939 source MCSA : MCSA4 56) chain C residue 595 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 57) chain C residue 608 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 58) chain C residue 544 type CROSSLNK sequence D description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 470 type CROSSLNK sequence D description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 60) chain C residue 481 type CROSSLNK sequence R description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 61) chain C residue 494 type CROSSLNK sequence K description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 source Swiss-Prot : SWS_FT_FI2 62) chain C residue 265 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4 63) chain C residue 914 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5

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