eF-site ID 1qru-A PDB Code 1qru Chain A click to enlarge Title GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA Classification LIGASE/RNA Compound TRNAGLN2 Source null (1QRU) Sequence A:  TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSI CLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEW LGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPE QTREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEE GKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCI YPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI TIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDD PRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASL ESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPN HPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGK EVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLGVIHW VSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVI KQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVF NRTVGLRDT Description Functional site 1) chain A residue 32 type sequence P description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 2) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 3) chain A residue 36 type sequence N description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 4) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 5) chain A residue 43 type sequence H description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 6) chain A residue 229 type sequence C description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 7) chain A residue 230 type sequence T description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 8) chain A residue 260 type sequence R description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 9) chain A residue 261 type sequence L description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 10) chain A residue 270 type sequence K description BINDING SITE FOR RESIDUE ATP A 999 source : AC1 11) chain A residue 231 type BINDING sequence L 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 12) chain A residue 261 type BINDING sequence L 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 13) chain A residue 269 type BINDING sequence S 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 14) chain A residue 35 type BINDING sequence P 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 15) chain A residue 41 type BINDING sequence I 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 16) chain A residue 67 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 17) chain A residue 212 type BINDING sequence D 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 18) chain A residue 35 type catalytic sequence P description 850 source MCSA : MCSA1 19) chain A residue 261 type catalytic sequence L description 850 source MCSA : MCSA1 20) chain A residue 271 type catalytic sequence R description 850 source MCSA : MCSA1 21) 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

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