eF-site ID 1tt5-ABCDEF PDB Code 1tt5 Chain A, B, C, D, E, F click to enlarge Title Structure of APPBP1-UBA3-Ubc12N26: a unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8 Classification CELL CYCLE, LIGASE Compound amyloid protein-binding protein 1 Source null (UBCM_HUMAN) Sequence A:  MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATA TGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSS IGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFF CRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVG YMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYD DHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLI RQGILKPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDD RCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDM IADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAP ESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEI ISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEE DIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHT IAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATF QL B:  MKLDWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDT CKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNL NRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQ DFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGV LDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYP PQVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFGEGVP LDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRI IPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVD GLYTYTFEAERKENCPACSQLPQNIQFLQEVLDYLTNSAS LQMKSPAITATNRTLYLQSVTSIEERTRPLSKGLVDGQEL AVADVTTPQTVLFK C:  LLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEIL KNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRA EAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVV VATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIII KEHPVIESHPDNALEDLRLDKPFPELREHFQSYHTPWIVI IAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKPEDE ENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTP SFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKL QNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKL LCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNE IVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLT GFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAA QEVIKIITKQFVIFNNTYIYSGMSQTSATFQL D:  WNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLVIGA GGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRP KDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYR QFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVP LIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMC TIASMPRLPEHCIEYVRMLQWPKEQPFGEGVPLDGDDPEH IQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTN AVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFE AERKENCPACSQLPQNIQLQEVLDYLTNSASLQMKSPAIT ATKNRTLYLQVTSIEERTRPLAVADVTTPQTVLFK E:  MIKLFSLKQQKKE F:  LFSLKQQKKE Description Functional site 1) chain B residue 199 type sequence C description BINDING SITE FOR RESIDUE ZN B 1014 source : AC1 2) chain B residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN B 1014 source : AC1 3) chain B residue 343 type sequence C description BINDING SITE FOR RESIDUE ZN B 1014 source : AC1 4) chain B residue 346 type sequence C description BINDING SITE FOR RESIDUE ZN B 1014 source : AC1 5) chain D residue 199 type sequence C description BINDING SITE FOR RESIDUE ZN D 1014 source : AC2 6) chain D residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN D 1014 source : AC2 7) chain D residue 343 type sequence C description BINDING SITE FOR RESIDUE ZN D 1014 source : AC2 8) chain D residue 346 type sequence C description BINDING SITE FOR RESIDUE ZN D 1014 source : AC2 9) chain A residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 10) chain C residue 346 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:Q8VBW6 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 216 type ACT_SITE sequence C description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 12) chain D residue 216 type ACT_SITE sequence C description Glycyl thioester intermediate source Swiss-Prot : SWS_FT_FI1 13) chain B residue 214-222 type prosite sequence PMCTIASMP description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PMCTIAsMP source prosite : PS00865 14) chain B residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 15) chain D residue 190 type SITE sequence R description Determines specificity for NEDD8 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2 19) chain D residue 127 type BINDING sequence I description BINDING => ECO:0000269|PubMed:14690597 source Swiss-Prot : SWS_FT_FI2

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