Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MPY

1.85 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus (IDP00699) in complex with NAD+

Replaces: 3FG0

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	33
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	ILE153
A	GLY217
A	PHE231
A	GLY233
A	GLY234
A	THR237
A	HIS240
A	ILE241
A	GLU255
A	GLY257
A	CME289
A	THR154
A	HIS336
A	LYS339
A	GLU390
A	PHE392
A	HOH674
A	HOH724
A	HOH819
A	HOH823
A	HOH867
A	HOH923
A	PRO155
A	HOH973
A	HOH998
A	HOH1030
A	HOH1038
A	TRP156
A	ASN157
A	LYS180
A	SER182
A	GLU183
A	GLY213

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

Chain	Residue
A	LYS460
A	GLY463
A	HOH648
B	VAL249
B	HOH726

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

Chain	Residue
A	ILE29
A	ASP97
A	ILE184
A	HOH843

site_id	AC4
Number of Residues	35
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	GLY233
B	GLY234
B	THR237
B	HIS240
B	ILE241
B	GLU255
B	GLY257
B	CME289
B	HIS336
B	LYS339
B	GLU390
B	PHE392
B	HOH643
B	HOH649
B	HOH734
B	HOH741
B	HOH809
B	HOH828
B	HOH855
B	HOH859
B	HOH1008
B	HOH1093

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 502

Chain	Residue
A	VAL249
A	HOH627
B	LYS460
B	GLY463
B	HOH674

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 503

Chain	Residue
B	ILE29
B	ASP97
B	ILE184
B	HOH676

site_id	AC7
Number of Residues	36
Details	BINDING SITE FOR RESIDUE NAD C 501

Chain	Residue
C	GLY233
C	GLY234
C	THR237
C	HIS240
C	GLU255
C	GLY257
C	CME289
C	HIS336
C	LYS339
C	GLU390
C	PHE392
C	HOH613
C	HOH663
C	HOH706
C	HOH720
C	HOH745
C	HOH801
C	HOH842
C	HOH929
C	HOH1047
C	HOH1126
C	HOH1159
C	HOH1187
C	ILE153
C	THR154
C	PRO155
C	TRP156
C	ASN157
C	GLN162
C	LYS180
C	SER182
C	GLU183
C	GLY213
C	GLY217
C	ASP218
C	PHE231

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 502

Chain	Residue
C	LYS460
C	GLY463
C	HOH641
D	VAL249
D	HOH667

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 503

Chain	Residue
C	ILE28
C	ILE29
C	ASP97
C	ILE184
C	HOH871

site_id	BC1
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAD D 501

Chain	Residue
D	ILE153
D	THR154
D	PRO155
D	TRP156
D	ASN157
D	LYS180
D	SER182
D	GLU183
D	GLY213
D	GLY217
D	ASP218
D	PHE231
D	GLY233
D	GLY234
D	THR237
D	HIS240
D	ILE241
D	GLU255
D	GLY257
D	CME289
D	HIS336
D	LYS339
D	GLU390
D	PHE392
D	HOH630
D	HOH758
D	HOH822
D	HOH873
D	HOH910
D	HOH929
D	HOH1085
D	HOH1124
D	HOH1153
D	HOH1167

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 502

Chain	Residue
C	VAL249
C	HOH718
D	LYS460
D	GLY463
D	HOH697

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 503

Chain	Residue
D	ILE29
D	ASP97
D	ILE184
D	HOH832

site_id	BC4
Number of Residues	36
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	GLY233
E	GLY234
E	THR237
E	HIS240
E	ILE241
E	GLU255
E	GLY257
E	CME289
E	HIS336
E	LYS339
E	GLU390
E	PHE392
E	HOH628
E	HOH678
E	HOH728
E	HOH770
E	HOH792
E	HOH806
E	HOH933
E	HOH965
E	HOH1079
E	HOH1214
E	HOH1225

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA E 502

Chain	Residue
E	NA503
E	HOH925
E	HOH993
F	HOH602
F	HOH605
F	HOH845
F	HOH1032

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA E 503

Chain	Residue
E	NA502
E	HOH925
E	HOH1050
E	HOH1227
F	HOH602
F	HOH845
F	HOH936

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA E 504

Chain	Residue
E	LYS460
E	GLY463
E	HOH619
F	VAL249
F	HOH666

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA E 505

Chain	Residue
E	ILE28
E	ILE29
E	ASP97
E	ILE184
E	HOH849

site_id	BC9
Number of Residues	37
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	PHE231
F	GLY233
F	GLY234
F	THR237
F	HIS240
F	ILE241
F	GLU255
F	GLY257
F	CME289
F	HIS336
F	LYS339
F	GLU390
F	PHE392
F	HOH616
F	HOH671
F	HOH692
F	HOH708
F	HOH729
F	HOH780
F	HOH809
F	HOH859
F	HOH976
F	HOH1169
F	HOH1200
F	HOH1217
F	HOH1235

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA F 502

Chain	Residue
C	SER342
C	HOH661
F	LEU7
F	GLN9
F	HOH765

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA F 503

Chain	Residue
F	ILE28
F	ILE29
F	ASP97
F	ILE184
F	HOH783

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA F 504

Chain	Residue
E	VAL249
E	HOH635
F	LYS460
F	GLY463
F	HOH670

site_id	CC4
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD G 501

Chain	Residue
G	ILE153
G	THR154
G	PRO155
G	TRP156
G	ASN157
G	LYS180
G	PRO181
G	SER182
G	GLU183
G	GLY213
G	GLY217
G	PHE231
G	GLY233
G	GLY234
G	THR237
G	HIS240
G	GLU255
G	GLY257
G	CME289
G	HIS336
G	LYS339
G	GLU390
G	PHE392
G	HOH692
G	HOH701
G	HOH845
G	HOH957
G	HOH983
G	HOH987
G	HOH991
G	HOH1148
G	HOH1152

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA G 502

Chain	Residue
G	LYS460
G	GLY463
G	HOH702
H	VAL249
H	HOH683

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA G 503

Chain	Residue
G	ILE29
G	ASP97
G	ILE184
G	HOH1062

site_id	CC7
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD H 501

Chain	Residue
H	ILE153
H	THR154
H	PRO155
H	TRP156
H	ASN157
H	LYS180
H	SER182
H	GLU183
H	GLY213
H	GLY217
H	PHE231
H	GLY233
H	GLY234
H	THR237
H	HIS240
H	ILE241
H	GLU255
H	GLY257
H	CME289
H	HIS336
H	LYS339
H	GLU390
H	PHE392
H	HOH717
H	HOH771
H	HOH785
H	HOH856
H	HOH887
H	HOH940
H	HOH1054
H	HOH1060
H	HOH1186

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA H 502

Chain	Residue
G	VAL249
G	HOH684
H	LYS460
H	GLY463
H	HOH699

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA H 503

Chain	Residue
H	ILE29
H	ASP97
H	ILE184
H	HOH947

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)