eF-site ID 4gqu-A PDB Code 4gqu Chain A click to enlarge Title Crystal structure of HisB from Mycobacterium tuberculosis Classification LYASE Compound Imidazoleglycerol-phosphate dehydratase Source Mycobacterium tuberculosis (HIS7_MYCTU) Sequence A:  SRRARIERRTRESDIVIELDLDGTGQVAVDTGVPFYDHML TALGSHASFDLTVRATGDVEIEAHHTIEDTAIALGTALGQ ALGDKRGIRRFGDAFIPMDETLAHAAVDLSGRPYCVHTGE PDHLQHTTIAGSSVPYHTVINRHVFESLAANARIALHVRV LYGRDPHHITEAQYKAVARALRQAVEPDPRV Description Functional site 1) chain A residue 73 type sequence H description BINDING SITE FOR RESIDUE MN A 301 source : AC1 2) chain A residue 77 type sequence E description BINDING SITE FOR RESIDUE MN A 301 source : AC1 3) chain A residue 152 type sequence H description BINDING SITE FOR RESIDUE MN A 301 source : AC1 4) chain A residue 177 type sequence H description BINDING SITE FOR RESIDUE MN A 301 source : AC1 5) chain A residue 47 type sequence H description BINDING SITE FOR RESIDUE MN A 302 source : AC2 6) chain A residue 74 type sequence H description BINDING SITE FOR RESIDUE MN A 302 source : AC2 7) chain A residue 176 type sequence H description BINDING SITE FOR RESIDUE MN A 302 source : AC2 8) chain A residue 180 type sequence E description BINDING SITE FOR RESIDUE MN A 302 source : AC2 9) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE MN A 303 source : AC3 10) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE MN A 303 source : AC3 11) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE MN A 303 source : AC3 12) chain A residue 151 type sequence R description BINDING SITE FOR RESIDUE MN A 304 source : AC4 13) chain A residue 128 type sequence G description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 14) chain A residue 151 type sequence R description BINDING SITE FOR RESIDUE EDO A 305 source : AC5 15) chain A residue 21 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:O23346 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 99 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23346 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:O23346 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 47 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 19) chain A residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 20) chain A residue 74 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 21) chain A residue 77 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 22) chain A residue 152 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 23) chain A residue 176 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 24) chain A residue 177 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 25) chain A residue 180 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24311587, ECO:0007744|PDB:4GQU source Swiss-Prot : SWS_FT_FI2 26) chain A residue 70-83 type prosite sequence IEAHHTIEDTAIAL description IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IEaHHtiEdtAIAL source prosite : PS00954 27) chain A residue 172-184 type prosite sequence GRDPHHITEAQYK description IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GrDpHHitEAqYK source prosite : PS00955

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