eF-site ID 1ile-A PDB Code 1ile Chain A click to enlarge Title ISOLEUCYL-TRNA SYNTHETASE Classification AMINOACYL-TRNA SYNTHETASE Compound ISOLEUCYL-TRNA SYNTHETASE Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (SYI_THET8) Sequence A:  MFKEVGEPNFPKLEEEVLAFWKREKIFQKSVENRKGGPRY TVYEGPPTANGLPHVGHAQARSYKDLFPRYKTMRGYYAPR RAGWDTHGLPVELEVEKKLGLKSKREIEAYGIERFNQACR ESVFTYEKEWEAFTERIAYWVDLEDAYATLEPTYIESIWW SLKNLFDRGLLYRDHKVVPYCPRCGTPLSSHEVALGYKEI QDPSVYVRFPLKEPKKLGLEKASLLIWTTTPWTLPGNVAA AVHPEYTYAAFQVGDEALILEEGLGRKLLGEGTQVLKTFP GKALEGLPYTPPYPQALEKGYFVVLADYVSQEDGTGIVHQ APAFGAEDLETARVYGLPLLKTVDEEGKLLVEPFKGLYFR EANRAILRDLRGRGLLFKEESYLHSYPHCWRCSTPLMYYA TESWFIKNTLFKDELIRNNQEIHWVPPHIKEGRYGEWLKN LVDWALSRNRYWGTPLPIWVCQACGKEEAIGSFQELKARA TKPLPEPFDPHRPYVDQVELACACGGTMRRVPYVIDVWYD SGAMPFASLHYPFEHEEVFRESFPADFIAEGIDQTRGWFN SLHQLGVMLFGSIAFKNVICHGLILDEKGQKMSKSKGNVV DPWDIIRKFGADALRWYIYVSAPPEADRRFGPNLVRETVR DYFLTLWNVYSFFVTYANLDRPDLKNPPPPEKRPEMDRWL LARMQDLIQRVTEALEAYDPTTSARALRDFVVEDLSQWYV RRNRRRFWKNEDALDREAAYATLYEALVLVATLAAPFTPF LAEVLWQNLVRSVRLEAKESVHLADWPEADPALADEALVA QMRAVLKVVDLARAARAKSGV Description (1)  ISOLEUCYL-TRNA SYNTHETASE Functional site 1) chain A residue 181 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 2) chain A residue 184 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 3) chain A residue 389 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 4) chain A residue 392 type sequence C description BINDING SITE FOR RESIDUE ZN A 1101 source : AC1 5) chain A residue 461 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 6) chain A residue 464 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 7) chain A residue 502 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 8) chain A residue 504 type sequence C description BINDING SITE FOR RESIDUE ZN A 1102 source : AC2 9) chain A residue 46 type catalytic sequence P description 309 source MCSA : MCSA1 10) chain A residue 85 type catalytic sequence D description 309 source MCSA : MCSA1 11) chain A residue 518 type catalytic sequence W description 309 source MCSA : MCSA1 12) chain A residue 554 type catalytic sequence Q description 309 source MCSA : MCSA1 13) chain A residue 558 type catalytic sequence W description 309 source MCSA : MCSA1 14) chain A residue 591 type catalytic sequence K description 309 source MCSA : MCSA1 15) chain A residue 594 type catalytic sequence K description 309 source MCSA : MCSA1 16) chain A residue 46 type BINDING sequence P description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 17) chain A residue 57 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 18) chain A residue 550 type BINDING sequence E description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 19) chain A residue 551 type BINDING sequence G description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 20) chain A residue 553 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 21) chain A residue 554 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 22) chain A residue 581 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11584022, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI1 23) chain A residue 181 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 24) chain A residue 184 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 25) chain A residue 389 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 26) chain A residue 392 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 27) chain A residue 502 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 28) chain A residue 504 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ, ECO:0007744|PDB:1JZS source Swiss-Prot : SWS_FT_FI2 29) chain A residue 319 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14672940 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 328 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672940 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 461 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE, ECO:0007744|PDB:1JZQ source Swiss-Prot : SWS_FT_FI4 32) chain A residue 464 type BINDING sequence C description BINDING => ECO:0007744|PDB:1ILE source Swiss-Prot : SWS_FT_FI5 33) chain A residue 594 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 47-58 type prosite sequence PTANGLPHVGHA description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PtaNGlPHVGHA source prosite : PS00178

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