Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4A0M

CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH IN COMPLEX WITH NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006081	biological_process	aldehyde metabolic 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	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0030955	molecular_function	potassium ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
A	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
A	0110095	biological_process	cellular detoxification of aldehyde
B	0006081	biological_process	aldehyde metabolic 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	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
B	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0030955	molecular_function	potassium ion binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
B	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
B	0110095	biological_process	cellular detoxification of aldehyde
C	0006081	biological_process	aldehyde metabolic 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	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
C	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0030955	molecular_function	potassium ion binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
C	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
C	0110095	biological_process	cellular detoxification of aldehyde
D	0006081	biological_process	aldehyde metabolic 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	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
D	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0030955	molecular_function	potassium ion binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
D	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
D	0110095	biological_process	cellular detoxification of aldehyde

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K D 1497

Chain	Residue
D	ILE28
D	ASP96
D	LEU186

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 1497

Chain	Residue
C	ILE28
C	ASP96
C	LEU186

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K B 1497

Chain	Residue
B	ASP96
B	LEU186

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 1497

Chain	Residue
A	ASP96
A	LEU186
A	ILE28

site_id	AC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD D 1498

Chain	Residue
D	ILE155
D	SER156
D	PRO157
D	TRP158
D	ASN159
D	LYS182
D	SER184
D	GLU185
D	GLY215
D	GLY219
D	ALA220
D	PHE233
D	THR234
D	GLY235
D	SER236
D	THR239
D	GLU257
D	LEU258
D	GLY259
D	CYS291
D	GLU390
D	PHE392
D	LEU418
D	TRP456
D	HOH2045
D	HOH2094
D	HOH2095

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD C 1498

Chain	Residue
C	ILE155
C	SER156
C	PRO157
C	TRP158
C	ASN159
C	LYS182
C	PRO183
C	SER184
C	GLU185
C	GLY215
C	GLY219
C	ALA220
C	PHE233
C	THR234
C	GLY235
C	SER236
C	THR239
C	GLU257
C	LEU258
C	GLY259
C	CYS291
C	GLU390
C	PHE392
C	LEU418
C	TRP456
C	HOH2061

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD B 1498

Chain	Residue
B	ILE155
B	SER156
B	PRO157
B	TRP158
B	ASN159
B	LYS182
B	PRO183
B	SER184
B	GLU185
B	GLY215
B	GLY219
B	ALA220
B	PHE233
B	THR234
B	GLY235
B	SER236
B	THR239
B	GLU257
B	GLY259
B	CYS291
B	GLU390
B	PHE392
B	TRP456
B	HOH2062
B	HOH2077
B	HOH2083
B	HOH2126
B	HOH2127
B	HOH2128
D	GLU138

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD A 1498

Chain	Residue
A	LYS182
A	SER184
A	GLU185
A	GLY215
A	GLY219
A	ALA220
A	PHE233
A	THR234
A	GLY235
A	SER236
A	THR239
A	GLU257
A	LEU258
A	GLY259
A	CYS291
A	GLU390
A	PHE392
A	LEU418
A	TRP456
A	HOH2074
A	HOH2166
A	HOH2167
A	HOH2168
A	ILE155
A	SER156
A	PRO157
A	TRP158
A	ASN159

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 1499

Chain	Residue
C	LEU477
C	ASN478
C	ILE479
D	PHE464
D	GLY465
D	ARG466
D	HOH2096

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 1500

Chain	Residue
D	TYR160
D	TRP167
D	CYS291
D	SER292
D	GLN448
D	CYS450
D	GOL1501

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 1501

Chain	Residue
D	ASP110
D	CYS450
D	PHE451
D	GOL1500

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 1499

Chain	Residue
C	ARG55
C	PHE58
C	LEU149
C	GLY150
C	ASP229
C	HOH2129
D	GLU438
D	LYS460

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 1502

Chain	Residue
C	LYS435
C	GLU438
D	GLN147
D	PRO148

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1499

Chain	Residue
A	TRP471
A	GLN474
B	ARG146
B	GLN474

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1500

Chain	Residue
A	GLN448
A	CYS450
A	HOH2170

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 1499

Chain	Residue
A	VAL251
A	PRO253
A	HOH2070
B	LYS460
B	GLY463
B	HOH2121

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 1501

Chain	Residue
A	LYS460
A	GLY463
A	HOH2149
B	VAL251
B	PRO253

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 1500

Chain	Residue
C	VAL251
C	PRO253
C	HOH2053
D	LYS460
D	GLY463

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1501

Chain	Residue
C	LYS460
C	GLY463
C	HOH2118
D	VAL251
D	PRO253
D	HOH2053

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE284-SER295

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

Chain	Residue	Details
A	LEU256-PRO263

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26792760","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A2D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V37","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26792760","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A2D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4V37","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Blocked amino end (Arg)"}

Chain

Residue

Details

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