eF-site ID 1mb2-D PDB Code 1mb2 Chain D 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 D:  MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIV DQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQ SEVPAHAQAAWMLQCIVYIGELERMTQFKEKSAGKEAVSA GLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAER FNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN LLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETL RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQ AMGLGR Description Functional site 1) chain D residue 5 type sequence F description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 2) chain D residue 7 type sequence G description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 3) chain D residue 9 type sequence Q description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 4) chain D residue 40 type sequence V description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 5) chain D residue 43 type sequence H description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 6) chain D residue 129 type sequence M description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 7) chain D residue 132 type sequence D description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 8) chain D residue 141 type sequence V description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 9) chain D residue 147 type sequence Q description BINDING SITE FOR RESIDUE TRP D 403 source : AC4 10) chain D residue 111 type catalytic sequence K description 481 source MCSA : MCSA4 11) chain D residue 192 type catalytic sequence K description 481 source MCSA : MCSA4 12) chain D residue 195 type catalytic sequence K description 481 source MCSA : MCSA4 13) chain D 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 14) chain D 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 15) chain D 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 16) chain D 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 17) chain D 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 18) chain D 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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