eF-site ID 4qto-ABCD PDB Code 4qto Chain A, B, C, D click to enlarge Title 1.65 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus with BME-modified Cys289 and PEG molecule in active site Classification OXIDOREDUCTASE Compound Betaine aldehyde dehydrogenase Source (Q5HCU0_STAAC) Sequence A:  AMELLKHLSQRQYIDGEWVESANKNTRDIINPYNQEVIFT VSEGTKEDAERAILAARRAFESGEWSQETAETRGKKVRAI ADKIKEHREALARLETLDTGKTLEESYADMDDIHNVFMYF AGLADKDGGEMIDSPIPDTESKIVKEPVGVVTQITPWNYP LLQASWKIAPALATGCSLVMKPSEITPLTTIRVFELMEEV GFPKGTINLILGAGSEVGDVMSGHKEVDLVSFTGGIETGK HIMKNAANNVTNIALELGGKNPNIIFDDADFELAVDQALN GGYFHAGQVXSAGSRILVQNSIKDKFEQALIDRVKKIKLG NGFDADTEMGPVISTEHRNKIESYMDVAKAEGATIAVGGK RPDRDDLKDGLFFEPTVITNCDTSMRIVQEEVFGPVVTVE GFETEQEAIQLANDSIYGLAGAVFSKDIGKAQRVANKLKL GTVWINDFHPYFAQAPWGGYKQSGIGRELGKEGLEEYLVS KHILTNTNPQLVNWFSK B:  AMELLKHLSQRQYIDGEWVESANKNTRDIINPYNQEVIFT VSEGTKEDAERAILAARRAFESGEWSQETAETRGKKVRAI ADKIKEHREALARLETLDTGKTLEESYADMDDIHNVFMYF AGLADKDGGEMIDSPIPDTESKIVKEPVGVVTQITPWNYP LLQASWKIAPALATGCSLVMKPSEITPLTTIRVFELMEEV GFPKGTINLILGAGSEVGDVMSGHKEVDLVSFTGGIETGK HIMKNAANNVTNIALELGGKNPNIIFDDADFELAVDQALN GGYFHAGQVXSAGSRILVQNSIKDKFEQALIDRVKKIKLG NGFDADTEMGPVISTEHRNKIESYMDVAKAEGATIAVGGK RPDRDDLKDGLFFEPTVITNCDTSMRIVQEEVFGPVVTVE GFETEQEAIQLANDSIYGLAGAVFSKDIGKAQRVANKLKL GTVWINDFHPYFAQAPWGGYKQSGIGRELGKEGLEEYLVS KHILTNTNPQLVNWFSK C:  MELLKHLSQRQYIDGEWVESANKNTRDIINPYNQEVIFTV SEGTKEDAERAILAARRAFESGEWSQETAETRGKKVRAIA DKIKEHREALARLETLDTGKTLEESYADMDDIHNVFMYFA GLADKDGGEMIDSPIPDTESKIVKEPVGVVTQITPWNYPL LQASWKIAPALATGCSLVMKPSEITPLTTIRVFELMEEVG FPKGTINLILGAGSEVGDVMSGHKEVDLVSFTGGIETGKH IMKNAANNVTNIALELGGKNPNIIFDDADFELAVDQALNG GYFHAGQVXSAGSRILVQNSIKDKFEQALIDRVKKIKLGN GFDADTEMGPVISTEHRNKIESYMDVAKAEGATIAVGGKR PDRDDLKDGLFFEPTVITNCDTSMRIVQEEVFGPVVTVEG FETEQEAIQLANDSIYGLAGAVFSKDIGKAQRVANKLKLG TVWINDFHPYFAQAPWGGYKQSGIGRELGKEGLEEYLVSK HILTNTNPQLVNWFSK D:  ELLKHLSQRQYIDGEWVESANKNTRDIINPYNQEVIFTVS EGTKEDAERAILAARRAFESGEWSQETAETRGKKVRAIAD KIKEHREALARLETLDTGKTLEESYADMDDIHNVFMYFAG LADKDGGEMIDSPIPDTESKIVKEPVGVVTQITPWNYPLL QASWKIAPALATGCSLVMKPSEITPLTTIRVFELMEEVGF PKGTINLILGAGSEVGDVMSGHKEVDLVSFTGGIETGKHI MKNAANNVTNIALELGGKNPNIIFDDADFELAVDQALNGG YFHAGQVXSAGSRILVQNSIKDKFEQALIDRVKKIKLGNG FDADTEMGPVISTEHRNKIESYMDVAKAEGATIAVGGKRP DRDDLKDGLFFEPTVITNCDTSMRIVQEEVFGPVVTVEGF ETEQEAIQLANDSIYGLAGAVFSKDIGKAQRVANKLKLGT VWINDFHPYFAQAPWGGYKQSGIGRELGKEGLEEYLVSKH ILTNTNPQLVNWFSK Description Functional site 1) chain A residue 460 type sequence K description BINDING SITE FOR RESIDUE NA A 501 source : AC1 2) chain A residue 463 type sequence G description BINDING SITE FOR RESIDUE NA A 501 source : AC1 3) chain B residue 249 type sequence V description BINDING SITE FOR RESIDUE NA A 501 source : AC1 4) chain A residue 283 type sequence F description BINDING SITE FOR RESIDUE PGE A 502 source : AC2 5) chain A residue 448 type sequence H description BINDING SITE FOR RESIDUE PGE A 502 source : AC2 6) chain A residue 450 type sequence Y description BINDING SITE FOR RESIDUE PGE A 502 source : AC2 7) chain A residue 342 type sequence S description BINDING SITE FOR RESIDUE PGE A 503 source : AC3 8) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE PGE A 503 source : AC3 9) chain A residue 346 type sequence V description BINDING SITE FOR RESIDUE PGE A 503 source : AC3 10) chain A residue 385 type sequence R description BINDING SITE FOR RESIDUE PGE A 503 source : AC3 11) chain A residue 8 type sequence S description BINDING SITE FOR RESIDUE PEG A 504 source : AC4 12) chain A residue 17 type sequence W description BINDING SITE FOR RESIDUE PEG A 504 source : AC4 13) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE PEG A 504 source : AC4 14) chain B residue 267 type sequence D description BINDING SITE FOR RESIDUE PEG A 504 source : AC4 15) chain B residue 268 type sequence A description BINDING SITE FOR RESIDUE PEG A 504 source : AC4 16) chain A residue 155 type sequence P description BINDING SITE FOR RESIDUE PEG A 505 source : AC5 17) chain A residue 234 type sequence G description BINDING SITE FOR RESIDUE PEG A 505 source : AC5 18) chain A residue 289 type sequence X description BINDING SITE FOR RESIDUE PEG A 505 source : AC5 19) chain A residue 336 type sequence H description BINDING SITE FOR RESIDUE PEG A 505 source : AC5 20) chain A residue 392 type sequence F description BINDING SITE FOR RESIDUE PEG A 505 source : AC5 21) chain A residue 61 type sequence S description BINDING SITE FOR RESIDUE PEG A 506 source : AC6 22) chain A residue 62 type sequence G description BINDING SITE FOR RESIDUE PEG A 506 source : AC6 23) chain A residue 63 type sequence E description BINDING SITE FOR RESIDUE PEG A 506 source : AC6 24) chain A residue 103 type sequence E description BINDING SITE FOR RESIDUE TRS A 507 source : AC7 25) chain A residue 324 type sequence A description BINDING SITE FOR RESIDUE TRS A 507 source : AC7 26) chain A residue 326 type sequence T description BINDING SITE FOR RESIDUE TRS A 507 source : AC7 27) chain A residue 327 type sequence E description BINDING SITE FOR RESIDUE TRS A 507 source : AC7 28) chain B residue 493 type sequence W description BINDING SITE FOR RESIDUE TRS A 507 source : AC7 29) chain A residue 249 type sequence V description BINDING SITE FOR RESIDUE NA B 501 source : AC8 30) chain B residue 460 type sequence K description BINDING SITE FOR RESIDUE NA B 501 source : AC8 31) chain B residue 463 type sequence G description BINDING SITE FOR RESIDUE NA B 501 source : AC8 32) chain B residue 107 type sequence A description BINDING SITE FOR RESIDUE PGE B 502 source : AC9 33) chain B residue 158 type sequence Y description BINDING SITE FOR RESIDUE PGE B 502 source : AC9 34) chain B residue 448 type sequence H description BINDING SITE FOR RESIDUE PGE B 502 source : AC9 35) chain B residue 450 type sequence Y description BINDING SITE FOR RESIDUE PGE B 502 source : AC9 36) chain B residue 66 type sequence Q description BINDING SITE FOR RESIDUE PEG B 503 source : BC1 37) chain B residue 67 type sequence E description BINDING SITE FOR RESIDUE PEG B 503 source : BC1 38) chain B residue 289 type sequence X description BINDING SITE FOR RESIDUE PEG B 504 source : BC2 39) chain B residue 336 type sequence H description BINDING SITE FOR RESIDUE PEG B 504 source : BC2 40) chain B residue 339 type sequence K description BINDING SITE FOR RESIDUE PEG B 504 source : BC2 41) chain B residue 392 type sequence F description BINDING SITE FOR RESIDUE PEG B 504 source : BC2 42) chain A residue 493 type sequence W description BINDING SITE FOR RESIDUE TRS B 505 source : BC3 43) chain B residue 103 type sequence E description BINDING SITE FOR RESIDUE TRS B 505 source : BC3 44) chain B residue 324 type sequence A description BINDING SITE FOR RESIDUE TRS B 505 source : BC3 45) chain B residue 326 type sequence T description BINDING SITE FOR RESIDUE TRS B 505 source : BC3 46) chain C residue 460 type sequence K description BINDING SITE FOR RESIDUE NA C 501 source : BC4 47) chain C residue 463 type sequence G description BINDING SITE FOR RESIDUE NA C 501 source : BC4 48) chain D residue 249 type sequence V description BINDING SITE FOR RESIDUE NA C 501 source : BC4 49) chain C residue 158 type sequence Y description BINDING SITE FOR RESIDUE PGE C 502 source : BC5 50) chain C residue 283 type sequence F description BINDING SITE FOR RESIDUE PGE C 502 source : BC5 51) chain C residue 448 type sequence H description BINDING SITE FOR RESIDUE PGE C 502 source : BC5 52) chain C residue 450 type sequence Y description BINDING SITE FOR RESIDUE PGE C 502 source : BC5 53) chain D residue 493 type sequence W description BINDING SITE FOR RESIDUE PGE C 502 source : BC5 54) chain C residue 342 type sequence S description BINDING SITE FOR RESIDUE PG4 C 503 source : BC6 55) chain C residue 343 type sequence Y description BINDING SITE FOR RESIDUE PG4 C 503 source : BC6 56) chain C residue 346 type sequence V description BINDING SITE FOR RESIDUE PG4 C 503 source : BC6 57) chain C residue 385 type sequence R description BINDING SITE FOR RESIDUE PG4 C 503 source : BC6 58) chain C residue 155 type sequence P description BINDING SITE FOR RESIDUE EDO C 504 source : BC7 59) chain C residue 233 type sequence G description BINDING SITE FOR RESIDUE EDO C 504 source : BC7 60) chain C residue 234 type sequence G description BINDING SITE FOR RESIDUE EDO C 504 source : BC7 61) chain C residue 289 type sequence X description BINDING SITE FOR RESIDUE EDO C 504 source : BC7 62) chain C residue 392 type sequence F description BINDING SITE FOR RESIDUE EDO C 504 source : BC7 63) chain C residue 249 type sequence V description BINDING SITE FOR RESIDUE NA D 501 source : BC8 64) chain D residue 460 type sequence K description BINDING SITE FOR RESIDUE NA D 501 source : BC8 65) chain D residue 463 type sequence G description BINDING SITE FOR RESIDUE NA D 501 source : BC8 66) chain D residue 158 type sequence Y description BINDING SITE FOR RESIDUE PGE D 502 source : BC9 67) chain D residue 448 type sequence H description BINDING SITE FOR RESIDUE PGE D 502 source : BC9 68) chain D residue 450 type sequence Y description BINDING SITE FOR RESIDUE PGE D 502 source : BC9 69) chain D residue 61 type sequence S description BINDING SITE FOR RESIDUE PEG D 503 source : CC1 70) chain D residue 62 type sequence G description BINDING SITE FOR RESIDUE PEG D 503 source : CC1 71) chain D residue 63 type sequence E description BINDING SITE FOR RESIDUE PEG D 503 source : CC1 72) chain A residue 282-293 type prosite sequence YFHAGQVXSAGS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YfHAGQVCSAGS source prosite : PS00070 73) chain A residue 254-261 type prosite sequence LELGGKNP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP source prosite : PS00687

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