eF-site ID 1e4l-AB PDB Code 1e4l Chain A, B click to enlarge Title Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZM Glu191Asp Classification HYDROLASE Compound BETA-GLUCOSIDASE, CHLOROPLASTIC Source Zea mays (Maize) (BGLC_MAIZE) Sequence A:  MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGES NWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMG MDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLE NGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYF AKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKR DDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLE PVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLN YYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIG PPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNV QGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKES AKWLKEFNTA B:  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 B residue 194 type sequence T description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 7) chain B residue 333 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 8) chain B residue 378 type sequence W description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 9) chain B residue 406 type sequence E description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 10) chain B residue 457 type sequence W description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 11) chain B residue 464 type sequence E description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 12) chain B residue 473 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 13) 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 14) 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 15) chain B 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 16) chain B 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 17) chain A residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 22) chain B residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 30) chain B residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 31) 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 32) chain B 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 33) chain A residue 402-410 type prosite sequence IYITENGIG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG source prosite : PS00572 34) 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

Display surface Download Links