eF-site ID 1hxj-A PDB Code 1hxj Chain A click to enlarge Title CRYSTAL STRUCTURE OF THE MAIZE ZM-P60.1 BETA-GLUCOSIDASE Classification HYDROLASE Compound BETA-GLUCOSIDASE Source Zea mays (Maize) (BGLC_MAIZE) Sequence A:  QMLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGE SNWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEM GMDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLL ENGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTY FAKVCFDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRC SPGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYK RDDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFL EPVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGL NYYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPI GPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIG DVDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSN VQGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKE SAKWLKEFNT Description Functional site 1) chain A residue 397-405 type prosite sequence IYITENGIG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG source prosite : PS00572 2) chain A residue 23-37 type prosite sequence FTFGAATSAYQIEGA description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA source prosite : PS00653 3) chain A residue 186 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 401 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 33 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI3 6) chain A residue 137 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 7) chain A residue 185 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 8) chain A residue 328 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 9) chain A residue 468 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 10) chain A residue 401 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 452 type BINDING sequence W description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6 12) chain A residue 459 type BINDING sequence E description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6

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