Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZWL

2.60 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) H448F/Y450L double mutant from Staphylococcus aureus in complex with NAD+ and BME-free Cys289

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
A	0070887	biological_process	cellular response to chemical stimulus
B	0000166	molecular_function	nucleotide binding
B	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
B	0070887	biological_process	cellular response to chemical stimulus
C	0000166	molecular_function	nucleotide binding
C	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
C	0070887	biological_process	cellular response to chemical stimulus
D	0000166	molecular_function	nucleotide binding
D	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
D	0070887	biological_process	cellular response to chemical stimulus
E	0000166	molecular_function	nucleotide binding
E	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
E	0070887	biological_process	cellular response to chemical stimulus
F	0000166	molecular_function	nucleotide binding
F	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
F	0070887	biological_process	cellular response to chemical stimulus
G	0000166	molecular_function	nucleotide binding
G	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
G	0070887	biological_process	cellular response to chemical stimulus
H	0000166	molecular_function	nucleotide binding
H	0008802	molecular_function	betaine-aldehyde dehydrogenase 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
H	0070887	biological_process	cellular response to chemical stimulus

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	GLY234
A	THR237
A	HIS240
A	GLU255
A	LEU256
A	THR154
A	GLY257
A	CYS289
A	GLU390
A	PHE392
A	LEU418
A	TRP456
A	HOH640
A	HOH648
A	HOH677
A	PRO155
A	TRP156
A	GLN162
A	LYS180
A	SER182
A	GLU183
A	GLY213

site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 502

Chain	Residue
A	ARG10
A	HOH674

site_id	AC3
Number of Residues	3
Details	binding site for residue SO4 A 503

Chain	Residue
A	ASN338
A	ARG360
C	LYS243

site_id	AC4
Number of Residues	31
Details	binding site for residue NAD B 501

Chain	Residue
B	ILE153
B	THR154
B	PRO155
B	TRP156
B	ASN157
B	LYS180
B	PRO181
B	SER182
B	GLU183
B	GLY213
B	GLY217
B	ASP218
B	PHE231
B	THR232
B	GLY233
B	GLY234
B	THR237
B	HIS240
B	ILE241
B	GLU255
B	LEU256
B	GLY257
B	CYS289
B	GLU390
B	PHE392
B	TRP456
B	HOH610
B	HOH623
B	HOH638
B	HOH642
B	HOH754

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 B 502

Chain	Residue
B	THR403
B	GLU404
G	LYS304

site_id	AC6
Number of Residues	3
Details	binding site for residue SO4 B 503

Chain	Residue
B	ASN338
B	ARG360
H	LYS367

site_id	AC7
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	PRO181
C	SER182
C	GLU183
C	GLY213
C	GLY217
C	PHE231
C	THR232
C	GLY233
C	GLY234
C	THR237
C	HIS240
C	GLU255
C	LEU256
C	GLY257
C	CYS289
C	GLU390
C	PHE392
C	TRP456
C	HOH630
C	HOH638
C	HOH664

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 C 502

Chain	Residue
G	LYS317
C	PRO202
C	LYS203

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 C 503

Chain	Residue
C	THR334
C	ARG337
C	ASN338
C	ARG360
C	HOH640

site_id	AD1
Number of Residues	27
Details	binding site for residue NAD D 501

Chain	Residue
D	ILE153
D	THR154
D	PRO155
D	TRP156
D	ASN157
D	GLN162
D	LYS180
D	SER182
D	GLU183
D	GLY213
D	GLY217
D	PHE231
D	THR232
D	GLY233
D	GLY234
D	THR237
D	HIS240
D	GLU255
D	LEU256
D	GLY257
D	CYS289
D	GLU390
D	PHE392
D	TRP456
D	HOH604
D	HOH613
D	HOH623

site_id	AD2
Number of Residues	3
Details	binding site for residue SO4 D 502

Chain	Residue
D	ARG337
D	ASN338
D	ARG360

site_id	AD3
Number of Residues	29
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	PHE231
E	THR232
E	GLY233
E	GLY234
E	THR237
E	HIS240
E	ILE241
E	GLU255
E	LEU256
E	GLY257
E	CYS289
E	GLU390
E	PHE392
E	LEU418
E	TRP456
E	HOH618
E	HOH631
E	HOH707

site_id	AD4
Number of Residues	4
Details	binding site for residue SO4 E 502

Chain	Residue
E	PHE265
E	GLN298
E	GLU404
E	LYS429

site_id	AD5
Number of Residues	2
Details	binding site for residue SO4 E 503

Chain	Residue
E	ASN338
E	ARG360

site_id	AD6
Number of Residues	28
Details	binding site for residue NAD F 501

Chain	Residue
F	ILE153
F	THR154
F	PRO155
F	TRP156
F	LYS180
F	SER182
F	GLU183
F	GLY213
F	GLY217
F	ASP218
F	PHE231
F	THR232
F	GLY233
F	GLY234
F	THR237
F	HIS240
F	GLU255
F	LEU256
F	GLY257
F	CYS289
F	GLU390
F	PHE392
F	TRP456
F	HOH601
F	HOH632
F	HOH667
F	HOH671
F	HOH727

site_id	AD7
Number of Residues	2
Details	binding site for residue SO4 F 502

Chain	Residue
F	LYS243
G	LYS243

site_id	AD8
Number of Residues	3
Details	binding site for residue SO4 F 503

Chain	Residue
F	ASN338
F	ARG360
H	LYS243

site_id	AD9
Number of Residues	1
Details	binding site for residue SO4 F 504

Chain	Residue
F	ARG10

site_id	AE1
Number of Residues	26
Details	binding site for residue NAD G 501

Chain	Residue
G	ILE153
G	THR154
G	PRO155
G	TRP156
G	GLN162
G	LYS180
G	SER182
G	GLU183
G	GLY213
G	GLY217
G	ASP218
G	PHE231
G	THR232
G	GLY233
G	GLY234
G	THR237
G	HIS240
G	GLU255
G	LEU256
G	GLY257
G	CYS289
G	GLU390
G	PHE392
G	LEU418
G	TRP456
G	HOH609

site_id	AE2
Number of Residues	4
Details	binding site for residue SO4 G 502

Chain	Residue
G	THR334
G	ARG337
G	ASN338
G	ARG360

site_id	AE3
Number of Residues	2
Details	binding site for residue SO4 G 503

Chain	Residue
C	ARG57
G	LYS314

site_id	AE4
Number of Residues	3
Details	binding site for residue SO4 G 504

Chain	Residue
D	SER342
G	ARG385
G	HOH647

site_id	AE5
Number of Residues	27
Details	binding site for residue NAD H 501

Chain	Residue
H	ILE153
H	THR154
H	PRO155
H	TRP156
H	ASN157
H	GLN162
H	LYS180
H	SER182
H	GLU183
H	GLY213
H	GLY217
H	PHE231
H	THR232
H	GLY233
H	GLY234
H	THR237
H	HIS240
H	GLU255
H	LEU256
H	GLY257
H	CYS289
H	GLU390
H	PHE392
H	LEU418
H	TRP456
H	HOH603
H	HOH618

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)