4Q92

1.90 Angstrom resolution crystal structure of apo betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) with BME-modified Cys289

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0006578	biological_process	amino-acid betaine biosynthetic process
A	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0006578	biological_process	amino-acid betaine biosynthetic process
B	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0006578	biological_process	amino-acid betaine biosynthetic process
C	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0006578	biological_process	amino-acid betaine biosynthetic process
D	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 501

Chain	Residue
A	GLY286
A	GLU390
A	GLY393
A	HOH644
A	HOH785
A	HOH956

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 502

Chain	Residue
B	VAL249
B	HOH912
A	LYS460
A	GLY463
A	HOH690

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 503

Chain	Residue
A	ARG77
A	ASP81
D	ASP81

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 501

Chain	Residue
A	VAL249
A	HOH978
B	LYS460
B	GLY463
B	HOH699

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 501

Chain	Residue
C	LYS460
C	GLY463
C	HOH646
D	VAL249
D	HOH645

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 502

Chain	Residue
C	GLY286
C	SER293
C	GLY393
C	HOH651
C	HOH1001
C	HOH1030

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site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 503

Chain	Residue
B	ASP81
C	ASP81

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site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 501

Chain	Residue
C	VAL249
C	HOH662
D	LYS460
D	GLY463
D	HOH608

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Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YfHAGQVCSAGS

Chain	Residue	Details
A	TYR282-SER293

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site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP

Chain	Residue	Details
A	LEU254-PRO261

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