eF-site ID 3j2t-ABCDEFGHIJKLMN PDB Code 3j2t Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N Title An improved model of the human apoptosome 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 QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE B:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE C:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE D:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE E:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE F:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE G:  GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLK GEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHW VSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAK DRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTT RDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQ LQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYT DLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLL FCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQF QRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENF QEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQA KQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFS EDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCA FSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTN SVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVK QFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLF DIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIR RLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGA IEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDD AEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLAT GDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLC FSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIH VSPDFKTYVTVDNLGILYILQTLE 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 Description (1)  Apoptotic protease-activating factor 1, Cytochrome c Functional site 1) chain A residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 2) chain A residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 3) chain A residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 4) chain A residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 5) chain A residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 6) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 7) chain A residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 8) chain A residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 9) chain A residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 10) chain A residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 11) chain A residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 12) chain A residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 13) chain A residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 14) chain A residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 15) chain A residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP A 1301 source : AC1 16) chain B residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 17) chain B residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 18) chain B residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 19) chain B residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 20) chain B residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 21) chain B residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 22) chain B residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 23) chain B residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 24) chain B residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 25) chain B residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 26) chain B residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 27) chain B residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 28) chain B residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 29) chain B residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 30) chain B residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP B 1301 source : AC2 31) chain C residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 32) chain C residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 33) chain C residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 34) chain C residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 35) chain C residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 36) chain C residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 37) chain C residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 38) chain C residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 39) chain C residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 40) chain C residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 41) chain C residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 42) chain C residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 43) chain C residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 44) chain C residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 45) chain C residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP C 1301 source : AC3 46) chain D residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 47) chain D residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 48) chain D residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 49) chain D residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 50) chain D residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 51) chain D residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 52) chain D residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 53) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 54) chain D residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 55) chain D residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 56) chain D residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 57) chain D residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 58) chain D residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 59) chain D residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 60) chain D residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP D 1301 source : AC4 61) chain E residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 62) chain E residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 63) chain E residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 64) chain E residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 65) chain E residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 66) chain E residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 67) chain E residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 68) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 69) chain E residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 70) chain E residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 71) chain E residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 72) chain E residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 73) chain E residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 74) chain E residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 75) chain E residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP E 1301 source : AC5 76) chain F residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 77) chain F residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 78) chain F residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 79) chain F residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 80) chain F residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 81) chain F residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 82) chain F residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 83) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 84) chain F residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 85) chain F residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 86) chain F residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 87) chain F residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 88) chain F residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 89) chain F residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 90) chain F residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP F 1301 source : AC6 91) chain G residue 125 type sequence V description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 92) chain G residue 126 type sequence F description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 93) chain G residue 127 type sequence V description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 94) chain G residue 129 type sequence R description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 95) chain G residue 155 type sequence M description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 96) chain G residue 157 type sequence G description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 97) chain G residue 158 type sequence C description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 98) chain G residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 99) chain G residue 160 type sequence K description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 100) chain G residue 161 type sequence S description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 101) chain G residue 162 type sequence V description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 102) chain G residue 294 type sequence I description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 103) chain G residue 321 type sequence P description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 104) chain G residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 105) chain G residue 325 type sequence S description BINDING SITE FOR RESIDUE ATP G 1301 source : AC7 106) chain H residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 107) chain H residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 108) chain H residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 109) chain H residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 110) chain H residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 111) chain H residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 112) chain H residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 113) chain H residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 114) chain H residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 115) chain H residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 116) chain H residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 117) chain H residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 118) chain H residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 119) chain H residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 120) chain H residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 121) chain H residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 122) chain H residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 123) chain H residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 124) chain H residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 125) chain H residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM H 500 source : AC8 126) chain I residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 127) chain I residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 128) chain I residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 129) chain I residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 130) chain I residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 131) chain I residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 132) chain I residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 133) chain I residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 134) chain I residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 135) chain I residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 136) chain I residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 137) chain I residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 138) chain I residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 139) chain I residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 140) chain I residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 141) chain I residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 142) chain I residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 143) chain I residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 144) chain I residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 145) chain I residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM I 500 source : AC9 146) chain J residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 147) chain J residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 148) chain J residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 149) chain J residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 150) chain J residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 151) chain J residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 152) chain J residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 153) chain J residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 154) chain J residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 155) chain J residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 156) chain J residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 157) chain J residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 158) chain J residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 159) chain J residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 160) chain J residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 161) chain J residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 162) chain J residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 163) chain J residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 164) chain J residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 165) chain J residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM J 500 source : BC1 166) chain K residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 167) chain K residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 168) chain K residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 169) chain K residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 170) chain K residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 171) chain K residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 172) chain K residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 173) chain K residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 174) chain K residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 175) chain K residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 176) chain K residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 177) chain K residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 178) chain K residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 179) chain K residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 180) chain K residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 181) chain K residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 182) chain K residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 183) chain K residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 184) chain K residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 185) chain K residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM K 500 source : BC2 186) chain L residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 187) chain L residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 188) chain L residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 189) chain L residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 190) chain L residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 191) chain L residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 192) chain L residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 193) chain L residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 194) chain L residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 195) chain L residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 196) chain L residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 197) chain L residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 198) chain L residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 199) chain L residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 200) chain L residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 201) chain L residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 202) chain L residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 203) chain L residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 204) chain L residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 205) chain L residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM L 500 source : BC3 206) chain M residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 207) chain M residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 208) chain M residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 209) chain M residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 210) chain M residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 211) chain M residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 212) chain M residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 213) chain M residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 214) chain M residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 215) chain M residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 216) chain M residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 217) chain M residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 218) chain M residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 219) chain M residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 220) chain M residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 221) chain M residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 222) chain M residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 223) chain M residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 224) chain M residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 225) chain M residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM M 500 source : BC4 226) chain N residue 13 type sequence K description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 227) chain N residue 14 type sequence C description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 228) chain N residue 16 type sequence Q description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 229) chain N residue 17 type sequence C description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 230) chain N residue 18 type sequence H description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 231) chain N residue 28 type sequence T description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 232) chain N residue 30 type sequence P description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 233) chain N residue 40 type sequence T description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 234) chain N residue 41 type sequence G description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 235) chain N residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 236) chain N residue 49 type sequence T description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 237) chain N residue 52 type sequence N description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 238) chain N residue 59 type sequence W description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 239) chain N residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 240) chain N residue 68 type sequence L description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 241) chain N residue 78 type sequence T description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 242) chain N residue 79 type sequence K description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 243) chain N residue 80 type sequence M description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 244) chain N residue 81 type sequence I description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 245) chain N residue 82 type sequence F description BINDING SITE FOR RESIDUE HEM N 500 source : BC5 246) chain A residue 672-686 type prosite sequence IATCSVDKKVKIWNS description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 247) chain A residue 716-730 type prosite sequence LATGSSDCFLKLWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 248) chain A residue 758-772 type prosite sequence LASCSADGTLKLWDA description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 249) chain A residue 1142-1156 type prosite sequence LATGDDNGEIRIWNV description WD_REPEATS_1 Trp-Asp (WD) repeats signature. IATCsvDkKVKIWNS source prosite : PS00678 250) chain H residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 251) chain L residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 252) chain M residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 253) chain M residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 254) chain N residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 255) chain N residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 256) chain H residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 257) chain I residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 258) chain I residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 259) chain J residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 260) chain J residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 261) chain K residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 262) chain K residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 263) chain L residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 264) chain H residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 265) chain I residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 266) chain J residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 267) chain K residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 268) chain L residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 269) chain M residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 270) chain N residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:5933874 source Swiss-Prot : SWS_FT_FI3 271) chain H residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 272) chain I residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 273) chain J residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 274) chain K residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 275) chain L residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 276) chain M residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 277) chain N residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16866357 source Swiss-Prot : SWS_FT_FI4 278) chain H residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 279) chain L residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 280) chain M residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 281) chain M residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 282) chain N residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 283) chain N residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 284) chain H residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 285) chain I residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 286) chain I residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 287) chain J residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 288) chain J residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 289) chain K residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 290) chain K residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2 291) chain L residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 292) chain H residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 293) chain I residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 294) chain J residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 295) chain K residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 296) chain L residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 297) chain M residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 298) chain N residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 299) chain H residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 300) chain I residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 301) chain J residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 302) chain K residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 303) chain L residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 304) chain M residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 305) chain N residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 306) chain H residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 307) chain I residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 308) chain J residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 309) chain K residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 310) chain L residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 311) chain M residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 312) chain N residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 313) chain H residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 314) chain I residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 315) chain J residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 316) chain K residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 317) chain L residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 318) chain M residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7 319) chain N residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:18471988 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links