eF-site ID 1euy-AB PDB Code 1euy Chain A, B click to enlarge Title GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR Classification ligase/RNA Compound GLUTAMINYL TRNA Source Escherichia coli (strain K12) (1EUY) Sequence A:  TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSI CLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEW LGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPE QIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEE GKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCI YPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI TIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDD PRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASL ESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPN HPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGK EVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLGVIHW VSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVI KQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVF NRTVGLRDT B:  GGGGUAUCGCCAAGCGGUAAGGCACCGGAUUCUGAUUCCG GCAAGCGAGGUUCGAAUCCUCGUACCCCAGCCA Description Functional site 1) chain A residue 30 type sequence R description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 2) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 3) chain A residue 32 type sequence P description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 4) chain A residue 33 type sequence P description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 5) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 6) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 7) chain A residue 43 type sequence H description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 8) chain A residue 46 type sequence S description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 9) chain A residue 66 type sequence D description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 10) chain A residue 211 type sequence Y description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 11) chain A residue 215 type sequence H description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 12) chain A residue 229 type sequence C description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 13) chain A residue 230 type sequence T description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 14) chain A residue 233 type sequence F description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 15) chain A residue 260 type sequence R description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 16) chain A residue 261 type sequence L description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 17) chain A residue 270 type sequence K description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 18) chain B residue 976 type sequence A description BINDING SITE FOR RESIDUE QSI A 998 source : AC1 19) chain A residue 34 type catalytic sequence E description 850 source MCSA : MCSA1 20) chain A residue 260 type catalytic sequence R description 850 source MCSA : MCSA1 21) chain A residue 270 type catalytic sequence K description 850 source MCSA : MCSA1 22) chain A residue 34 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ source Swiss-Prot : SWS_FT_FI1 23) chain A residue 40 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ source Swiss-Prot : SWS_FT_FI1 24) chain A residue 211 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1ZJW source Swiss-Prot : SWS_FT_FI3 25) chain A residue 230 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ source Swiss-Prot : SWS_FT_FI4 26) chain A residue 260 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ source Swiss-Prot : SWS_FT_FI4 27) chain A residue 268 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ source Swiss-Prot : SWS_FT_FI4 28) chain A residue 33-44 type prosite sequence PEPNGYLHIGHA description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGyLHIGHA source prosite : PS00178 29) chain A residue 66 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B source Swiss-Prot : SWS_FT_FI2

Display surface Download Links