eF-site ID 5juy-ABCDEFGHIJKLMNOPQR PDB Code 5juy Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R Title Active human apoptosome with procaspase-9 Classification APOPTOSIS Compound Apoptotic protease-activating factor 1 Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTS GLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNT DSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLW ETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLI NGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILE LVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQV WNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKV WNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTA KIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNG EIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDG KMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDF KTYVTVDNLGILYILQTLE B:  MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEE EKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY KDLAALLHDGIPVVSGITSYVRTVLCEGGVPQRPVVFVTR KKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVR DHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQD ESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSW VLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKE KGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGA LLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMS ISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETE EVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKN CSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAY HMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEY RHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLC EPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRL VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEK LLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTG ELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWD LNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKL WDATSANERKSINVKQFFLNEDMEVIVKCCSWSADGARIM VAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHL AVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDG SSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENE VMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQ YIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTAD EKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLK NSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDIS HDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSA FSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAA THGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFY TNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE C:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTS GLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNT DSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLW ETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLI NGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILE LVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQV WNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKV WNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTA KIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNG EIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDG KMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDF KTYVTVDNLGILYILQTLE D:  MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEE EKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY KDLAALLHDGIPVVSGITSYVRTVLCEGGVPQRPVVFVTR KKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVR DHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQD ESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSW VLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKE KGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGA LLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMS ISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETE EVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKN CSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAY HMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEY RHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLC EPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRL VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEK LLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTG ELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWD LNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKL WDATSANERKSINVKQFFLNEDMEVIVKCCSWSADGARIM VAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHL AVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDG SSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENE VMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQ YIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTAD EKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLK NSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDIS HDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSA FSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAA THGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFY TNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE E:  MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEE EKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY KDLAALLHDGIPVVSGITSYVRTVLCEGGVPQRPVVFVTR KKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVR DHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQD ESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSW VLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKE KGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGA LLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMS ISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETE EVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKN CSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAY HMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEY RHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLC EPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRL VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEK LLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTG ELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWD LNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKL WDATSANERKSINVKQFFLNEDMEVIVKCCSWSADGARIM VAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHL AVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDG SSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENE VMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQ YIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTAD EKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLK NSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDIS HDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSA FSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAA THGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFY TNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE F:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTS GLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNT DSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLW ETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLI NGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILE LVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQV WNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKV WNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTA KIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNG EIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDG KMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDF KTYVTVDNLGILYILQTLE G:  MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEE EKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY KDLAALLHDGIPVVSGITSYVRTVLCEGGVPQRPVVFVTR KKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVR DHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQD ESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSW VLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKE KGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGA LLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMS ISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETE EVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKN CSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAY HMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEY RHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLC EPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRL VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEK LLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTG ELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWD LNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKL WDATSANERKSINVKQFFLNEDMEVIVKCCSWSADGARIM VAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHL AVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDG SSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENE VMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQ YIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTAD EKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLK NSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDIS HDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSA FSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAA THGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFY TNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE H:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE I:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE J:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE K:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE L:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE M:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE N:  GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKM IFAGIKKKGEREDLIAYLKKATNE O:  MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMI EDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDT GQDMLASFLRTNRQA P:  MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMI EDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDT GQDMLASFLRTNRQA Q:  MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMI EDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDT GQDMLASFLRTNRQA R:  MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMI EDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDT GQDMLASFLRTNRQA Description (1)  Apoptotic protease-activating factor 1, Cytochrome c, Caspase-9 (E.C.3.4.22.62) Functional site 1) chain A residue 672-686 type prosite sequence IATCSVDKKVKIWNS description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 2) chain A residue 716-730 type prosite sequence LATGSSDCFLKLWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 3) chain A residue 758-772 type prosite sequence LASCSADGTLKLWDA description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 4) chain A residue 1142-1156 type prosite sequence LATGDDNGEIRIWNV description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 5) chain H residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 6) chain I residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 7) chain J residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 8) chain K residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 9) chain L residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 10) chain M residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 11) chain N residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 12) chain J residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 13) chain J residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 14) chain K residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 15) chain K residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 16) chain L residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 17) chain H residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 18) chain H residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 19) chain I residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 20) chain I residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 21) chain L residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 22) chain M residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 23) chain M residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 24) chain N residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 25) chain N residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 26) chain I residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 27) chain J residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 28) chain J residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 29) chain K residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 30) chain K residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 31) chain L residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 32) chain H residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 33) chain H residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 34) chain I residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 35) chain L residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 36) chain M residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 37) chain M residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 38) chain N residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 39) chain N residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 40) chain H residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 41) chain I residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 42) chain J residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 43) chain K residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 44) chain L residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 45) chain M residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 46) chain N residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 47) chain I residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 48) chain J residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 49) chain K residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 50) chain L residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 51) chain M residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 52) chain N residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 53) chain H residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 54) chain H residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 55) chain I residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 56) chain J residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 57) chain K residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 58) chain L residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 59) chain M residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 60) chain N residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 61) chain H residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 62) chain I residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 63) chain J residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 64) chain K residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 65) chain L residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 66) chain M residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 67) chain N residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 68) chain H residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 69) chain I residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 70) chain J residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 71) chain K residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 72) chain L residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 73) chain M residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 74) chain N residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7

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