eF-site ID 1mb2-A PDB Code 1mb2 Chain A click to enlarge Title Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation Classification LIGASE Compound TRYPTOPHAN-TRNA LIGASE Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (SYW_BACST) Sequence A:  MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIV DQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQ SEVPAHAQAAWMLQCIVYIGELERMTQFKEKSAGKEAVSA GLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAER FNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN LLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETL RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQ AMGLGR Description Functional site 1) chain A residue 5 type sequence F description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 2) chain A residue 7 type sequence G description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 3) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 4) chain A residue 43 type sequence H description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 5) chain A residue 129 type sequence M description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 6) chain A residue 132 type sequence D description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 7) chain A residue 143 type sequence V description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 8) chain A residue 147 type sequence Q description BINDING SITE FOR RESIDUE TRP A 400 source : AC1 9) chain A residue 111 type catalytic sequence K description 481 source MCSA : MCSA1 10) chain A residue 192 type catalytic sequence K description 481 source MCSA : MCSA1 11) chain A residue 195 type catalytic sequence K description 481 source MCSA : MCSA1 12) chain A residue 9 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 17 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 132 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 183 type BINDING sequence I description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 192 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 10-19 type prosite sequence PSGVITIGNY description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY source prosite : PS00178

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