eF-site ID 1e4l-A PDB Code 1e4l Chain A click to enlarge Title Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZM Glu191Asp Classification HYDROLASE Compound BETA-GLUCOSIDASE, CHLOROPLASTIC Source null (BGLC_MAIZE) Sequence A:  MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGES NWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMG MDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLE NGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYF AKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKR DDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLE PVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLN YYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIG PPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNV QGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKES AKWLKEFNTA Description Functional site 1) chain A residue 333 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1001 source : AC1 2) chain A residue 406 type sequence E description BINDING SITE FOR RESIDUE GOL A 1001 source : AC1 3) chain A residue 457 type sequence W description BINDING SITE FOR RESIDUE GOL A 1001 source : AC1 4) chain A residue 464 type sequence E description BINDING SITE FOR RESIDUE GOL A 1001 source : AC1 5) chain A residue 465 type sequence W description BINDING SITE FOR RESIDUE GOL A 1001 source : AC1 6) chain A residue 457 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 7) chain A residue 464 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 8) chain A residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 9) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 10) chain A residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 38 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 15) chain A residue 402-410 type prosite sequence IYITENGIG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG source prosite : PS00572 16) chain A residue 28-42 type prosite sequence FTFGAATSAYQIEGA description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA source prosite : PS00653 17) chain A residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links