eF-site ID 2nvu-ABCIJ PDB Code 2nvu Chain A, B, C, I, J click to enlarge Title Structure of APPBP1-UBA3~NEDD8-NEDD8-MgATP-Ubc12(C111A), a trapped ubiquitin-like protein activation complex Classification PROTEIN TURNOVER, LIGASE Compound NEDD8-activating enzyme E1 regulatory subunit Source Homo sapiens (Human) (NEDD8_HUMAN) Sequence A:  GKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTE ILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKN RAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFT VVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRI IIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHM EKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFR DLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSS IEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLP VRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKL LQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGL DTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPG VSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCR YGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSG MSQTSATFQL B:  KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKVALKSYEEEATMENAQKGEIMPN IPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAADW EGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLV IGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFL FRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDT FYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSS IVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNF PMCTIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDGDD PEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVA STNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTY TFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSAS LQMKSPAITATLEGKNRTLYLQSVTSIEERTRPNLSKTLK ELGLVDGQELAVADVTTPQTVLFKLHFTS C:  KLFSLKQQKKEEEKGSSKKASAAQLRIQKDINELNLPKTC DISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYP HDPPKVKCETMVYHPNIDLEGNVALNILREDWKPVLTINS IIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRS MRGGYIGSTYFERCLK I:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG J:  MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQ QRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGG Description Functional site 1) chain B residue 2146 type sequence D description BINDING SITE FOR RESIDUE MG B 101 source : AC1 2) chain B residue 2199 type sequence C description BINDING SITE FOR RESIDUE ZN B 102 source : AC2 3) chain B residue 2202 type sequence C description BINDING SITE FOR RESIDUE ZN B 102 source : AC2 4) chain B residue 2343 type sequence C description BINDING SITE FOR RESIDUE ZN B 102 source : AC2 5) chain B residue 2346 type sequence C description BINDING SITE FOR RESIDUE ZN B 102 source : AC2 6) chain A residue 15 type sequence R description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 7) chain B residue 2056 type sequence A description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 8) chain B residue 2057 type sequence G description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 9) chain B residue 2079 type sequence D description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 10) chain B residue 2080 type sequence M description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 11) chain B residue 2081 type sequence D description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 12) chain B residue 2087 type sequence N description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 13) chain B residue 2090 type sequence R description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 14) chain B residue 2091 type sequence Q description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 15) chain B residue 2103 type sequence K description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 16) chain B residue 2125 type sequence N description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 17) chain B residue 2126 type sequence K description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 18) chain B residue 2127 type sequence I description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 19) chain B residue 2128 type sequence Q description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 20) chain B residue 2144 type sequence G description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 21) chain B residue 2146 type sequence D description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 22) chain I residue 76 type sequence G description BINDING SITE FOR RESIDUE ATP B 103 source : AC3 23) chain I residue 27-52 type prosite sequence KERVEEKEGIPPQQQRLIYSGKQMND description UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD source prosite : PS00299 24) chain B residue 2214-2222 type prosite sequence PMCTIASMP description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PMCTIAsMP source prosite : PS00865 25) chain B residue 1108-1125 type prosite sequence PIAVEALSLIYNKDLLPN description SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN source prosite : PS01037 26) chain I residue 8 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 27) chain I residue 44 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 28) chain J residue 8 type SITE sequence L description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 29) chain J residue 44 type SITE sequence I description Interaction with UBE1C => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI1 30) chain I residue 40 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 31) chain J residue 40 type MOD_RES sequence Q description (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597 source Swiss-Prot : SWS_FT_FI2 32) chain I residue 48 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 33) chain J residue 48 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29595 source Swiss-Prot : SWS_FT_FI3 34) chain I residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 35) chain J residue 76 type CROSSLNK sequence G description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) source Swiss-Prot : SWS_FT_FI4 36) chain C residue 174 type MOD_RES sequence G description Omega-N-methylarginine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI5

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