Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QJE

1.85 Angstrom resolution crystal structure of apo betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) with BME-free sulfinic acid form of Cys289

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
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	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
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	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
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	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
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	4
Details	BINDING SITE FOR RESIDUE NA A 501

Chain	Residue
A	ILE29
A	ASP97
A	ILE184
A	HOH856

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

Chain	Residue
A	LYS460
A	GLY463
A	HOH612
B	VAL249
B	HOH728

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 503

Chain	Residue
A	SER61
A	GLY62
A	GLU63
A	GLN66

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 504

Chain	Residue
A	SER342
A	TYR343
A	VAL346
A	ARG385
A	HOH1016

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 505

Chain	Residue
A	GLU103
A	ALA324
A	THR326
A	HOH655
A	HOH1095
A	HOH1152
B	TRP493

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 501

Chain	Residue
B	ILE29
B	ASP97
B	ILE184
B	HOH777

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 502

Chain	Residue
A	VAL249
A	HOH657
B	LYS460
B	GLY463
B	HOH621

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 503

Chain	Residue
B	GLY62
B	GLU63
B	GLN66

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 501

Chain	Residue
C	ILE29
C	ASP97
C	ILE184
C	HOH763

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 502

Chain	Residue
C	LYS460
C	GLY463
C	HOH618
D	VAL249
D	HOH662

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG C 503

Chain	Residue
C	ASN487

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 504

Chain	Residue
C	SER342
C	TYR343
C	VAL346
C	ARG385
C	HOH1023

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 505

Chain	Residue
C	GLY62
C	GLU63
C	GLU67
C	HOH969

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS C 506

Chain	Residue
C	TRP493
C	HOH643
C	HOH972
C	HOH1140
D	GLU103
D	ALA324
D	THR326

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS C 507

Chain	Residue
C	GLU103
C	ALA324
C	THR326
C	HOH725
C	HOH1029
C	HOH1080
D	TRP493

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE B3P C 508

Chain	Residue
C	TRP17
C	ARG191
C	GLU194
C	GLU197
C	GLU198
C	HOH663
C	HOH839
C	HOH895
C	HOH1150
C	HOH1185
C	HOH1221

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 501

Chain	Residue
D	ILE29
D	ASP97
D	ILE184
D	HOH800

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 502

Chain	Residue
C	VAL249
C	HOH657
D	LYS460
D	GLY463
D	HOH632

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG D 503

Chain	Residue
D	GLY62
D	GLU63
D	GLN66
D	HOH1073
D	HOH1204

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
B	TYR282-SER293

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

Chain	Residue	Details
A	LEU254-PRO261
B	LEU254-PRO261

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)