eF-site ID 1hxj-AB PDB Code 1hxj Chain A, B 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 B:  SEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGESNWDH FCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMGMDAY RFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLENGIE PYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYFAKVC FDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRCSPGLD CAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKRDDTR IGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLEPVVR GDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLNYYTS RFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIGPPMG NPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGDVDTK ETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNVQGYF AWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKESAKWL KEFNTAKKPSKK Description Functional site 1) chain A residue 186 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 186 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 401 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 401 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 5) 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 6) 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 7) chain B 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 8) chain B 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 9) 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 10) chain B 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 11) chain A residue 397-405 type prosite sequence IYITENGIG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG source prosite : PS00572 12) 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 13) chain A residue 401 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 401 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 137 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 185 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 328 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 468 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 137 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 185 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 328 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 468 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4

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