eF-site ID 3h0m-ABCDEFGHIJKLMNOPQRSTUVWX PDB Code 3h0m Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X Title Structure of trna-dependent amidotransferase gatcab from aquifex aeolicus Classification LIGASE Compound Glutamyl-tRNA(Gln) amidotransferase subunit A Source Aquifex aeolicus (GATC_AQUAE) Sequence A:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT B:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL C:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV D:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT E:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL F:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV G:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT H:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL I:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV J:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT K:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL L:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV M:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT N:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL O:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV P:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT Q:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL R:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV S:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT T:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL U:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV V:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT W:  EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPV CLGMPGALPIVNKRAVEYAIRASLALNCEVHEESVFARKH YFYPDLPKGYQISQYEKPLATNGWVELNLPNGEKKKVRIR RLHIEEDAGKNIHEGDKTLVDLNRAGTPLMEIVTEPDIRT PEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGG EVVQETRTFDPQTGKTYPMRTKEEAEDYRYFPDPDLVPLK VKKEWIEEIKKNMPELPDQRFERLIKEYGLSEYEAGILVN HKEVGDFFEEAVRHFKEPKGIVNWLINDLLGLLRDKGISI EESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT PSQIVEEKGL X:  VDREWVLKIAKLARLELKEEEIEVFQKQLSDILDFIDQLK ELDTENVEPYIQEFEETPMREDEPHPSLDREKALMNAPER KDGFFVVPRVV Description Functional site 1) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 2) chain A residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 3) chain A residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 4) chain A residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 5) chain A residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 6) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 7) chain A residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 8) chain A residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 9) chain A residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 10) chain A residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 11) chain A residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 12) chain A residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 13) chain A residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 14) chain A residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN A 901 source : AC1 15) chain D residue 121 type sequence A description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 16) chain D residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 17) chain D residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 18) chain D residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 19) chain D residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 20) chain D residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 21) chain D residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 22) chain D residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 23) chain D residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 24) chain D residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 25) chain D residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 26) chain D residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 27) chain D residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 28) chain D residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN D 902 source : AC2 29) chain G residue 121 type sequence A description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 30) chain G residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 31) chain G residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 32) chain G residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 33) chain G residue 147 type sequence S description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 34) chain G residue 166 type sequence S description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 35) chain G residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 36) chain G residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 37) chain G residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 38) chain G residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 39) chain G residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 40) chain G residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 41) chain G residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 42) chain G residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN G 903 source : AC3 43) chain J residue 121 type sequence A description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 44) chain J residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 45) chain J residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 46) chain J residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 47) chain J residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 48) chain J residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 49) chain J residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 50) chain J residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 51) chain J residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 52) chain J residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 53) chain J residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 54) chain J residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 55) chain J residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN J 904 source : AC4 56) chain M residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 57) chain M residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 58) chain M residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 59) chain M residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 60) chain M residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 61) chain M residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 62) chain M residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 63) chain M residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 64) chain M residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 65) chain M residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 66) chain M residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 67) chain M residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN M 905 source : AC5 68) chain P residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 69) chain P residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 70) chain P residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 71) chain P residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 72) chain P residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 73) chain P residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 74) chain P residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 75) chain P residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 76) chain P residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 77) chain P residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 78) chain P residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 79) chain P residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 80) chain P residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN P 906 source : AC6 81) chain S residue 121 type sequence A description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 82) chain S residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 83) chain S residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 84) chain S residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 85) chain S residue 147 type sequence S description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 86) chain S residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 87) chain S residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 88) chain S residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 89) chain S residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 90) chain S residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 91) chain S residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 92) chain S residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 93) chain S residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN S 907 source : AC7 94) chain V residue 122 type sequence M description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 95) chain V residue 123 type sequence G description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 96) chain V residue 124 type sequence S description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 97) chain V residue 167 type sequence D description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 98) chain V residue 168 type sequence T description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 99) chain V residue 169 type sequence G description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 100) chain V residue 170 type sequence G description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 101) chain V residue 171 type sequence S description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 102) chain V residue 199 type sequence F description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 103) chain V residue 302 type sequence Y description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 104) chain V residue 303 type sequence Y description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 105) chain V residue 351 type sequence R description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 106) chain V residue 418 type sequence D description BINDING SITE FOR RESIDUE GLN V 908 source : AC8 107) chain B residue 14 type sequence H description BINDING SITE FOR RESIDUE MG B 479 source : AC9 108) chain B residue 127 type sequence E description BINDING SITE FOR RESIDUE MG B 479 source : AC9 109) chain B residue 153 type sequence E description BINDING SITE FOR RESIDUE MG B 479 source : AC9 110) chain H residue 14 type sequence H description BINDING SITE FOR RESIDUE MG H 479 source : BC1 111) chain H residue 127 type sequence E description BINDING SITE FOR RESIDUE MG H 479 source : BC1 112) chain H residue 153 type sequence E description BINDING SITE FOR RESIDUE MG H 479 source : BC1 113) chain K residue 14 type sequence H description BINDING SITE FOR RESIDUE MG K 479 source : BC2 114) chain K residue 127 type sequence E description BINDING SITE FOR RESIDUE MG K 479 source : BC2 115) chain K residue 153 type sequence E description BINDING SITE FOR RESIDUE MG K 479 source : BC2 116) chain N residue 14 type sequence H description BINDING SITE FOR RESIDUE MG N 479 source : BC3 117) chain N residue 127 type sequence E description BINDING SITE FOR RESIDUE MG N 479 source : BC3 118) chain N residue 153 type sequence E description BINDING SITE FOR RESIDUE MG N 479 source : BC3 119) chain Q residue 14 type sequence H description BINDING SITE FOR RESIDUE MG Q 479 source : BC4 120) chain Q residue 127 type sequence E description BINDING SITE FOR RESIDUE MG Q 479 source : BC4 121) chain Q residue 153 type sequence E description BINDING SITE FOR RESIDUE MG Q 479 source : BC4 122) chain T residue 14 type sequence H description BINDING SITE FOR RESIDUE MG T 479 source : BC5 123) chain T residue 127 type sequence E description BINDING SITE FOR RESIDUE MG T 479 source : BC5 124) chain T residue 153 type sequence E description BINDING SITE FOR RESIDUE MG T 479 source : BC5 125) chain W residue 14 type sequence H description BINDING SITE FOR RESIDUE MG W 479 source : BC6 126) chain W residue 127 type sequence E description BINDING SITE FOR RESIDUE MG W 479 source : BC6 127) chain W residue 153 type sequence E description BINDING SITE FOR RESIDUE MG W 479 source : BC6 128) chain B residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : BC7 129) chain B residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : BC7 130) chain B residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : BC7 131) chain B residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN B 901 source : BC7 132) chain E residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN E 902 source : BC8 133) chain E residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN E 902 source : BC8 134) chain E residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN E 902 source : BC8 135) chain E residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN E 902 source : BC8 136) chain H residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN H 903 source : BC9 137) chain H residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN H 903 source : BC9 138) chain H residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN H 903 source : BC9 139) chain H residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN H 903 source : BC9 140) chain K residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN K 904 source : CC1 141) chain K residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN K 904 source : CC1 142) chain K residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN K 904 source : CC1 143) chain K residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN K 904 source : CC1 144) chain N residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN N 905 source : CC2 145) chain N residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN N 905 source : CC2 146) chain N residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN N 905 source : CC2 147) chain N residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN N 905 source : CC2 148) chain Q residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN Q 906 source : CC3 149) chain Q residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN Q 906 source : CC3 150) chain Q residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN Q 906 source : CC3 151) chain Q residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN Q 906 source : CC3 152) chain T residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN T 907 source : CC4 153) chain T residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN T 907 source : CC4 154) chain T residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN T 907 source : CC4 155) chain T residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN T 907 source : CC4 156) chain W residue 25 type sequence C description BINDING SITE FOR RESIDUE ZN W 908 source : CC5 157) chain W residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN W 908 source : CC5 158) chain W residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN W 908 source : CC5 159) chain W residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN W 908 source : CC5 160) chain A residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 161) chain M residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 162) chain P residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 163) chain P residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 164) chain S residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 165) chain S residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 166) chain V residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 167) chain V residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 168) chain A residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 169) chain D residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 170) chain D residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 171) chain G residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 172) chain G residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 173) chain J residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 174) chain J residue 147 type ACT_SITE sequence S description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 175) chain M residue 72 type ACT_SITE sequence K description Charge relay system => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 176) chain A residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 177) chain D residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 178) chain G residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 179) chain J residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 180) chain M residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 181) chain P residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 182) chain S residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 183) chain V residue 171 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 184) chain A residue 145-176 type prosite sequence GGSSGGSAASVAVLSAPVSLGSDTGGSIRQPA description AMIDASES Amidases signature. GGSSGGsAAsVAvlsapvSlGsDtGgSIRqPA source prosite : PS00571 185) chain B residue 144-158 type prosite sequence LNRAGTPLMEIVTEP description GATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LNRagtPLMEIvTeP source prosite : PS01234

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