eF-site ID 1sr9-A PDB Code 1sr9 Chain A click to enlarge Title Crystal Structure of LeuA from Mycobacterium tuberculosis Classification TRANSFERASE Compound 2-isopropylmalate synthase Source (LEU1_MYCTU) Sequence A:  TIVKPAGPPRVGQPSWNPQRASSXPVNRYRPFAEEVEPIR LRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPXSPARKRR XFDLLVRXGYKEIEVGFPSASQTDFDFVREIIEQGAIPDD VTIQVLTQCRPELIERTFQACSGAPRAIVHFYNSTSILQR RVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSP ESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEX TTPNVYADSIEWXSRNLANRESVILSLHPHNDRGTAVAAA ELGFAAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVD PQIDFSNIDEIRRTVEYCNQLPVHERHPYGGDLVYTAFSG SHQDAINKGLDAXKLDADAADCDVDDXLWQVPYLPIDPRD VGRTYEAVIKGGVAYIXKTDHGLSLPRRLQIEFSQVIQKI EVSPKEXWDAFAEEYLAPVRPLERIRQHVDAADDDGGTTS ITATVKINGVETEISGSGNGPLAAFVHALADVGFDVAVLD YYEHAXSAGDDAQAAAYVEASVTISKTVWGVGIAPSITTA SLRAVVSAVNRAA Description (1)  2-isopropylmalate synthase(E.C.2.3.3.13) Functional site 1) chain A residue 81 type sequence D description BINDING SITE FOR RESIDUE ZN A 704 source : AC2 2) chain A residue 285 type sequence H description BINDING SITE FOR RESIDUE ZN A 704 source : AC2 3) chain A residue 287 type sequence H description BINDING SITE FOR RESIDUE ZN A 704 source : AC2 4) chain A residue 533 type sequence G description BINDING SITE FOR RESIDUE CL A 705 source : AC3 5) chain A residue 534 type sequence P description BINDING SITE FOR RESIDUE CL A 705 source : AC3 6) chain A residue 535 type sequence L description BINDING SITE FOR RESIDUE CL A 705 source : AC3 7) chain A residue 80 type sequence R description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 8) chain A residue 81 type sequence D description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 9) chain A residue 167 type sequence H description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 10) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 11) chain A residue 218 type sequence E description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 12) chain A residue 252 type sequence P description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 13) chain A residue 254 type sequence T description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 14) chain A residue 285 type sequence H description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 15) chain A residue 287 type sequence H description BINDING SITE FOR RESIDUE KIV A 701 source : AC4 16) chain A residue 80 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159544, ECO:0000269|PubMed:22352945, ECO:0000312|PDB:1SR9, ECO:0000312|PDB:3U6W source Swiss-Prot : SWS_FT_FI1 17) chain A residue 254 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15159544, ECO:0000269|PubMed:22352945, ECO:0000312|PDB:1SR9, ECO:0000312|PDB:3U6W source Swiss-Prot : SWS_FT_FI1 18) chain A residue 81 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:15159544, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:1SR9, ECO:0007744|PDB:3FIG, ECO:0007744|PDB:3HPS, ECO:0007744|PDB:3HPX, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1, ECO:0007744|PDB:3U6W source Swiss-Prot : SWS_FT_FI2 19) chain A residue 285 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:15159544, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:1SR9, ECO:0007744|PDB:3FIG, ECO:0007744|PDB:3HPS, ECO:0007744|PDB:3HPX, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1, ECO:0007744|PDB:3U6W source Swiss-Prot : SWS_FT_FI2 20) chain A residue 287 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:15159544, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:1SR9, ECO:0007744|PDB:3FIG, ECO:0007744|PDB:3HPS, ECO:0007744|PDB:3HPX, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1, ECO:0007744|PDB:3U6W source Swiss-Prot : SWS_FT_FI2 21) chain A residue 321 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 532 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 23) chain A residue 536 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 24) chain A residue 563 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 25) chain A residue 565 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 26) chain A residue 625 type BINDING sequence P description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 27) chain A residue 627 type BINDING sequence I description BINDING => ECO:0000269|PubMed:15159544, ECO:0000312|PDB:3FIG source Swiss-Prot : SWS_FT_FI4 28) chain A residue 79-95 type prosite sequence LRDGNQALIDPXSPARK description AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGnQalidPmsparK source prosite : PS00815 29) chain A residue 282-295 type prosite sequence LSLHPHNDRGTAVA description AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. LslHpHNDrGtAvA source prosite : PS00816

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