Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QN2

2.6 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) in complex with NAD+ and BME-free Cys289

Replaces: 4NI4

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
E	0000166	molecular_function	nucleotide binding
E	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
E	0006578	biological_process	amino-acid betaine biosynthetic process
E	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
E	0016491	molecular_function	oxidoreductase activity
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E	0019285	biological_process	glycine betaine biosynthetic process from choline
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
F	0006578	biological_process	amino-acid betaine biosynthetic process
F	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
F	0016491	molecular_function	oxidoreductase activity
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0019285	biological_process	glycine betaine biosynthetic process from choline
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
G	0006578	biological_process	amino-acid betaine biosynthetic process
G	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
G	0016491	molecular_function	oxidoreductase activity
G	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G	0019285	biological_process	glycine betaine biosynthetic process from choline
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
H	0006578	biological_process	amino-acid betaine biosynthetic process
H	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
H	0016491	molecular_function	oxidoreductase activity
H	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H	0019285	biological_process	glycine betaine biosynthetic process from choline
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	ILE153
A	GLY217
A	ASP218
A	PHE231
A	THR232
A	GLY233
A	SER234
A	THR237
A	HIS240
A	ILE241
A	GLU255
A	THR154
A	LEU256
A	GLY257
A	CYS289
A	GLU390
A	PHE392
A	LEU418
A	TRP456
A	HOH654
A	HOH678
A	PRO155
A	TRP156
A	ASN157
A	LYS180
A	SER182
A	GLU183
A	GLY213

site_id	AC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD B 501

Chain	Residue
B	ILE153
B	THR154
B	PRO155
B	TRP156
B	ASN157
B	GLN162
B	LYS180
B	SER182
B	GLU183
B	GLY213
B	GLY217
B	ASP218
B	PHE231
B	THR232
B	GLY233
B	SER234
B	THR237
B	HIS240
B	ILE241
B	GLU255
B	LEU256
B	GLY257
B	CYS289
B	GLU390
B	PHE392
B	LEU418
B	TRP456
B	HOH602
B	HOH709

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 502

Chain	Residue
A	GLU271
B	GLU103
B	ALA324
B	THR326
H	TRP493

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD C 501

Chain	Residue
C	ILE153
C	THR154
C	PRO155
C	TRP156
C	ASN157
C	LYS180
C	SER182
C	GLU183
C	GLY213
C	GLY217
C	ASP218
C	PHE231
C	THR232
C	GLY233
C	SER234
C	THR237
C	HIS240
C	ILE241
C	GLU255
C	LEU256
C	GLY257
C	CYS289
C	GLU390
C	PHE392
C	LEU418
C	TRP456
C	HOH608

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD D 501

Chain	Residue
D	ASP218
D	PHE231
D	THR232
D	GLY233
D	SER234
D	THR237
D	HIS240
D	ILE241
D	GLU255
D	LEU256
D	GLY257
D	CYS289
D	GLU390
D	PHE392
D	LEU418
D	TRP456
D	HOH622
D	HOH689
D	HOH704
D	ILE153
D	THR154
D	PRO155
D	TRP156
D	ASN157
D	LYS180
D	SER182
D	GLU183
D	GLY213
D	GLY217

site_id	AC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD E 501

Chain	Residue
E	ILE153
E	THR154
E	PRO155
E	TRP156
E	ASN157
E	GLN162
E	LYS180
E	SER182
E	GLU183
E	GLY213
E	GLY217
E	ASP218
E	PHE231
E	THR232
E	GLY233
E	SER234
E	THR237
E	HIS240
E	GLU255
E	LEU256
E	GLY257
E	CYS289
E	GLU390
E	PHE392
E	LEU418
E	TRP456
E	HOH606
E	HOH657

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD F 501

Chain	Residue
F	ILE153
F	THR154
F	PRO155
F	TRP156
F	ASN157
F	GLN162
F	LYS180
F	SER182
F	GLU183
F	GLY213
F	GLY217
F	ASP218
F	PHE231
F	THR232
F	GLY233
F	SER234
F	THR237
F	HIS240
F	GLU255
F	LEU256
F	GLY257
F	CYS289
F	GLU390
F	PHE392
F	LEU418
F	TRP456
F	HOH612
F	HOH619

site_id	AC8
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD G 501

Chain	Residue
G	ILE153
G	THR154
G	PRO155
G	TRP156
G	ASN157
G	LYS180
G	SER182
G	GLU183
G	GLY213
G	GLY217
G	ASP218
G	PHE231
G	THR232
G	GLY233
G	SER234
G	THR237
G	HIS240
G	GLU255
G	LEU256
G	GLY257
G	CYS289
G	GLU390
G	PHE392
G	LEU418
G	TRP456
G	HOH613
G	HOH681

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD H 501

Chain	Residue
H	ILE153
H	THR154
H	PRO155
H	TRP156
H	ASN157
H	LYS180
H	PRO181
H	SER182
H	GLU183
H	GLY213
H	GLY217
H	ASP218
H	PHE231
H	THR232
H	GLY233
H	SER234
H	THR237
H	HIS240
H	GLU255
H	LEU256
H	GLY257
H	CYS289
H	GLU390
H	PHE392
H	LEU418
H	TRP456
H	HOH603
H	HOH630
H	HOH635

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

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

Chain	Residue	Details
A	LEU254-PRO261

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