eF-site ID 1e4l-B PDB Code 1e4l Chain 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 B:  MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGES NWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMG MDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLE NGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYF AKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKR DDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLE PVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLN YYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIG PPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNV QGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKES AKWLKEFNTA Description Functional site 1) chain B residue 194 type sequence T description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 2) chain B residue 333 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 3) chain B residue 378 type sequence W description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 4) chain B residue 406 type sequence E description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 5) chain B residue 457 type sequence W description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 6) chain B residue 464 type sequence E description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 7) chain B residue 473 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1001 source : AC2 8) chain B residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 10) 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 11) chain B residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 16) 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 17) 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

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