Structure of PDB 4qn2 Chain B

Receptor sequence
>4qn2B (length=496) Species: 93062 (Staphylococcus aureus subsp. aureus COL) [Search protein sequence]
MELLKHLSQRQYIDGEWVESANKNTRDIINPYNQEVIFTVSEGTKEDAER
AILAARRAFESGEWSQETAETRGKKVRAIADKIKEHREALARLETLDTGK
TLEESYADMDDIHNVFMYFAGLADKDGGEMIDSPIPDTESKIVKEPVGVV
TQITPWNYPLLQASWKIAPALATGCSLVMKPSEITPLTTIRVFELMEEVG
FPKGTINLILGAGSEVGDVMSGHKEVDLVSFTGSIETGKHIMKNAANNVT
NIALELGGKNPNIIFDDADFELAVDQALNGGYFHAGQVCSAGSRILVQNS
IKDKFEQALIDRVKKIKLGNGFDADTEMGPVISTEHRNKIESYMDVAKAE
GATIAVGGKRPDRDDLKDGLFFEPTVITNCDTSMRIVQEEVFGPVVTVEG
FETEQEAIQLANDSIYGLAGAVFSKDIGKAQRVANKLKLGTVWINDFHPY
FAQAPWGGYKQSGIGRELGKEGLEEYLVSKHILTNTNPQLVNWFSK
3D structure
PDB4qn2 Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N157 K180 E255 C289 E390 E467
Catalytic site (residue number reindexed from 1) N157 K180 E255 C289 E390 E467
Enzyme Commision number 1.2.1.8: betaine-aldehyde dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD B I153 T154 P155 W156 N157 Q162 K180 S182 E183 G213 G217 F231 T232 G233 S234 T237 H240 I241 E255 L256 C289 E390 F392 L418 W456 I153 T154 P155 W156 N157 Q162 K180 S182 E183 G213 G217 F231 T232 G233 S234 T237 H240 I241 E255 L256 C289 E390 F392 L418 W456
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008802 betaine-aldehyde dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0006578 amino-acid betaine biosynthetic process
GO:0019285 glycine betaine biosynthetic process from choline

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4qn2, PDBe:4qn2, PDBj:4qn2
PDBsum4qn2
PubMed25945581
UniProtA0A0H2X0S3

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