eF-site ID 1mb2-CF PDB Code 1mb2 Chain C, F click to enlarge Title Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Tryptophan in an Open Conformation Classification LIGASE Compound TRYPTOPHAN-TRNA LIGASE Source null (SYW_BACST) Sequence C:  MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIV DQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQ SEVPAHAQAAWMLQCIVYIGELERMTQFKEKSAGKEAVSA GLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAER FNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN LLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETL RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQ AMGLGR F:  MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIV DQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQ SEVPAHAQAAWMLQCIVYIGELERMTQFKEKSAGKEAVSA GLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAER FNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN LLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETL RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQ AMGLGR Description Functional site 1) chain C residue 5 type sequence F description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 2) chain C residue 7 type sequence G description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 3) chain C residue 40 type sequence V description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 4) chain C residue 43 type sequence H description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 5) chain C residue 129 type sequence M description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 6) chain C residue 132 type sequence D description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 7) chain C residue 143 type sequence V description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 8) chain C residue 147 type sequence Q description BINDING SITE FOR RESIDUE TRP C 402 source : AC3 9) chain F residue 5 type sequence F description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 10) chain F residue 7 type sequence G description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 11) chain F residue 9 type sequence Q description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 12) chain F residue 43 type sequence H description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 13) chain F residue 129 type sequence M description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 14) chain F residue 132 type sequence D description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 15) chain F residue 143 type sequence V description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 16) chain F residue 147 type sequence Q description BINDING SITE FOR RESIDUE TRP F 405 source : AC6 17) chain C residue 111 type catalytic sequence K description 481 source MCSA : MCSA3 18) chain C residue 192 type catalytic sequence K description 481 source MCSA : MCSA3 19) chain C residue 195 type catalytic sequence K description 481 source MCSA : MCSA3 20) chain F residue 111 type catalytic sequence K description 481 source MCSA : MCSA6 21) chain F residue 192 type catalytic sequence K description 481 source MCSA : MCSA6 22) chain F residue 195 type catalytic sequence K description 481 source MCSA : MCSA6 23) chain C 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 24) chain C 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 25) chain C 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 26) chain C 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 27) chain F 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 28) chain F 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 29) chain F 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 30) chain F 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 31) chain F 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 32) chain F 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 33) chain C 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 34) chain C 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

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