eF-site ID 4qf6-ABCDEFGHIJKL PDB Code 4qf6 Chain A, B, C, D, E, F, G, H, I, J, K, L Title Structure of Aldehyde Dehydrogenase from Bacillus cereus, E194S mutant Classification OXIDOREDUCTASE Compound Aldehyde dehydrogenase Source Bacillus cereus ATCC 10876 (C2N217_BACCE) Sequence A:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK B:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK C:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK D:  IELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPATE DVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERAH LIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISATV ENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQII PWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAAK LFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTGS TVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEAI NGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMAN NVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGATV AAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVVV LPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKLK AGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYTE VKSVWVNIK E:  NIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPAT EDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERA HLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISAT VENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQI IPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAA KLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTG STVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEA INGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMA NNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGAT VAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVV VLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKL KAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYT EVKSVWVNIK F:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK G:  NIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPAT EDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERA HLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISAT VENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQI IPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAA KLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTG STVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEA INGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMA NNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGAT VAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVV VLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKL KAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYT EVKSVWVNIK H:  NIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPAT EDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERA HLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISAT VENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQI IPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAA KLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTG STVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEA INGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMA NNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGAT VAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVV VLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKL KAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYT EVKSVWVNIK I:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK J:  TNIELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPA TEDVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAER AHLIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISA TVENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQ IIPWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYA AKLFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFT GSTVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEE AINGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKM ANNVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGA TVAAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVV VVLPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANK LKAGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNY TEVKSVWVNIK K:  IELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPATE DVLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERAH LIYKLADLIEEHREELAQLEALDNGKPYQVALDDDISATV ENYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQII PWNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAAK LFKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTGS TVTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEAI NGAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMAN NVKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGATV AAGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVVV LPFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKLK AGTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYTE VKSVWVNIK L:  ELKPKVEAFLNEEIKMFINGEFVSAIGGKTFETYNPATED VLAVVCEAQEEDIDAAVKAARSAFESGPWAEMTTAERAHL IYKLADLIEEHREELAQLEALDNGKPYQVALDDDISATVE NYRYYAGWTTKIIGQTIPISKDYLNYTRHEPVGVVGQIIP WNFPLVMSSWKMGAALATGCTIVLKPASQTPLSLLYAAKL FKEAGFPNGVVNFVPGFGPEAGAAIVNHHDIDKVAFTGST VTGKYIMRQSAEMIKHVTLELGGKSPNIILEDADLEEAIN GAFQGIMYNHGQNCSAGSRVFVHRKHYETVVDALVKMANN VKLGAGMEKETEMGPLVSKKQQERVLNYIEQGKKEGATVA AGGERALEKGYFVKPTVFTDVTDDMTIVKEEIFGPVVVVL PFDSTEEVIERANNSSYGLAAGVWTQNIKTGHQVANKLKA GTVWINDYNLENAAAPFGGYKQSGIGRELGSYALDNYTEV KSVWVNIK Description Functional site 1) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE NA A 501 source : AC1 2) chain A residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA A 501 source : AC1 3) chain A residue 108 type sequence D description BINDING SITE FOR RESIDUE NA A 501 source : AC1 4) chain A residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA A 501 source : AC1 5) chain A residue 467 type sequence K description BINDING SITE FOR RESIDUE NA A 502 source : AC2 6) chain A residue 470 type sequence G description BINDING SITE FOR RESIDUE NA A 502 source : AC2 7) chain C residue 260 type sequence I description BINDING SITE FOR RESIDUE NA A 502 source : AC2 8) chain B residue 39 type sequence T description BINDING SITE FOR RESIDUE NA B 501 source : AC3 9) chain B residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA B 501 source : AC3 10) chain B residue 108 type sequence D description BINDING SITE FOR RESIDUE NA B 501 source : AC3 11) chain B residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA B 501 source : AC3 12) chain B residue 467 type sequence K description BINDING SITE FOR RESIDUE NA B 502 source : AC4 13) chain B residue 470 type sequence G description BINDING SITE FOR RESIDUE NA B 502 source : AC4 14) chain I residue 260 type sequence I description BINDING SITE FOR RESIDUE NA B 502 source : AC4 15) chain C residue 39 type sequence T description BINDING SITE FOR RESIDUE NA C 501 source : AC5 16) chain C residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA C 501 source : AC5 17) chain C residue 108 type sequence D description BINDING SITE FOR RESIDUE NA C 501 source : AC5 18) chain C residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA C 501 source : AC5 19) chain A residue 260 type sequence I description BINDING SITE FOR RESIDUE NA C 502 source : AC6 20) chain C residue 467 type sequence K description BINDING SITE FOR RESIDUE NA C 502 source : AC6 21) chain C residue 470 type sequence G description BINDING SITE FOR RESIDUE NA C 502 source : AC6 22) chain D residue 467 type sequence K description BINDING SITE FOR RESIDUE NA D 501 source : AC7 23) chain D residue 470 type sequence G description BINDING SITE FOR RESIDUE NA D 501 source : AC7 24) chain E residue 260 type sequence I description BINDING SITE FOR RESIDUE NA D 501 source : AC7 25) chain D residue 39 type sequence T description BINDING SITE FOR RESIDUE NA D 502 source : AC8 26) chain D residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA D 502 source : AC8 27) chain D residue 108 type sequence D description BINDING SITE FOR RESIDUE NA D 502 source : AC8 28) chain D residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA D 502 source : AC8 29) chain E residue 39 type sequence T description BINDING SITE FOR RESIDUE NA E 501 source : AC9 30) chain E residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA E 501 source : AC9 31) chain E residue 108 type sequence D description BINDING SITE FOR RESIDUE NA E 501 source : AC9 32) chain E residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA E 501 source : AC9 33) chain D residue 260 type sequence I description BINDING SITE FOR RESIDUE NA E 502 source : BC1 34) chain E residue 467 type sequence K description BINDING SITE FOR RESIDUE NA E 502 source : BC1 35) chain E residue 470 type sequence G description BINDING SITE FOR RESIDUE NA E 502 source : BC1 36) chain F residue 39 type sequence T description BINDING SITE FOR RESIDUE NA F 501 source : BC2 37) chain F residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA F 501 source : BC2 38) chain F residue 108 type sequence D description BINDING SITE FOR RESIDUE NA F 501 source : BC2 39) chain F residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA F 501 source : BC2 40) chain F residue 467 type sequence K description BINDING SITE FOR RESIDUE NA F 502 source : BC3 41) chain F residue 470 type sequence G description BINDING SITE FOR RESIDUE NA F 502 source : BC3 42) chain J residue 260 type sequence I description BINDING SITE FOR RESIDUE NA F 502 source : BC3 43) chain G residue 467 type sequence K description BINDING SITE FOR RESIDUE NA G 501 source : BC4 44) chain G residue 470 type sequence G description BINDING SITE FOR RESIDUE NA G 501 source : BC4 45) chain H residue 260 type sequence I description BINDING SITE FOR RESIDUE NA G 501 source : BC4 46) chain G residue 39 type sequence T description BINDING SITE FOR RESIDUE NA G 502 source : BC5 47) chain G residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA G 502 source : BC5 48) chain G residue 108 type sequence D description BINDING SITE FOR RESIDUE NA G 502 source : BC5 49) chain G residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA G 502 source : BC5 50) chain H residue 39 type sequence T description BINDING SITE FOR RESIDUE NA H 501 source : BC6 51) chain H residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA H 501 source : BC6 52) chain H residue 108 type sequence D description BINDING SITE FOR RESIDUE NA H 501 source : BC6 53) chain H residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA H 501 source : BC6 54) chain G residue 260 type sequence I description BINDING SITE FOR RESIDUE NA H 502 source : BC7 55) chain H residue 467 type sequence K description BINDING SITE FOR RESIDUE NA H 502 source : BC7 56) chain H residue 470 type sequence G description BINDING SITE FOR RESIDUE NA H 502 source : BC7 57) chain I residue 39 type sequence T description BINDING SITE FOR RESIDUE NA I 501 source : BC8 58) chain I residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA I 501 source : BC8 59) chain I residue 108 type sequence D description BINDING SITE FOR RESIDUE NA I 501 source : BC8 60) chain I residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA I 501 source : BC8 61) chain B residue 260 type sequence I description BINDING SITE FOR RESIDUE NA I 502 source : BC9 62) chain I residue 467 type sequence K description BINDING SITE FOR RESIDUE NA I 502 source : BC9 63) chain I residue 470 type sequence G description BINDING SITE FOR RESIDUE NA I 502 source : BC9 64) chain J residue 39 type sequence T description BINDING SITE FOR RESIDUE NA J 501 source : CC1 65) chain J residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA J 501 source : CC1 66) chain J residue 108 type sequence D description BINDING SITE FOR RESIDUE NA J 501 source : CC1 67) chain J residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA J 501 source : CC1 68) chain F residue 260 type sequence I description BINDING SITE FOR RESIDUE NA J 502 source : CC2 69) chain J residue 467 type sequence K description BINDING SITE FOR RESIDUE NA J 502 source : CC2 70) chain J residue 470 type sequence G description BINDING SITE FOR RESIDUE NA J 502 source : CC2 71) chain K residue 39 type sequence T description BINDING SITE FOR RESIDUE NA K 501 source : CC3 72) chain K residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA K 501 source : CC3 73) chain K residue 108 type sequence D description BINDING SITE FOR RESIDUE NA K 501 source : CC3 74) chain K residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA K 501 source : CC3 75) chain K residue 467 type sequence K description BINDING SITE FOR RESIDUE NA K 502 source : CC4 76) chain K residue 470 type sequence G description BINDING SITE FOR RESIDUE NA K 502 source : CC4 77) chain L residue 260 type sequence I description BINDING SITE FOR RESIDUE NA K 502 source : CC4 78) chain L residue 39 type sequence T description BINDING SITE FOR RESIDUE NA L 501 source : CC5 79) chain L residue 40 type sequence Y description BINDING SITE FOR RESIDUE NA L 501 source : CC5 80) chain L residue 108 type sequence D description BINDING SITE FOR RESIDUE NA L 501 source : CC5 81) chain L residue 195 type sequence Q description BINDING SITE FOR RESIDUE NA L 501 source : CC5 82) chain K residue 260 type sequence I description BINDING SITE FOR RESIDUE NA L 502 source : CC6 83) chain L residue 467 type sequence K description BINDING SITE FOR RESIDUE NA L 502 source : CC6 84) chain L residue 470 type sequence G description BINDING SITE FOR RESIDUE NA L 502 source : CC6 85) chain A residue 265-272 type prosite sequence LELGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP source prosite : PS00687

Display surface Download Links