Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4V3F

Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with betaine aldehyde

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	2
Details	BINDING SITE FOR RESIDUE IOD A 1499

Chain	Residue
A	HIS143
B	THR434

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 1500

Chain	Residue
A	LYS21
A	ASN23

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 1501

Chain	Residue
A	GLN474

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHT A 1502

Chain	Residue
A	GLN448
A	CYS450
A	TYR160
A	TRP167
A	ILE290
A	SER292

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 A 1503

Chain	Residue
A	TRP471
A	GLN474
B	GLU470
B	TRP471

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 1498

Chain	Residue
A	GLU431
B	HIS143

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 1499

Chain	Residue
B	LYS128

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 1500

Chain	Residue
A	HOH2186
B	GLY465

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHT B 1501

Chain	Residue
B	TYR160
B	TRP167
B	CSO291
B	GLN448
B	CYS450

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1502

Chain	Residue
B	CYS450
B	PHE451
B	HOH2121

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 1498

Chain	Residue
C	HIS143

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 1499

Chain	Residue
C	GLN474

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 C 1500

Chain	Residue
C	TRP471
D	GLU470
D	TRP471

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ETX C 1501

Chain	Residue
C	THR378
C	ASP379
C	ILE380
C	VAL398
C	HOH2128

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD D 1498

Chain	Residue
C	THR434
D	LYS130
D	HIS143

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD D 1500

Chain	Residue
D	ARG146

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHT D 1501

Chain	Residue
D	TYR160
D	ILE290
D	CSO291
D	GLN448
D	CYS450

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PG4 D 1502

Chain	Residue
C	LEU149
C	VAL251
C	PRO253
C	LEU477
C	ILE479
D	GLY458
D	ILE459
D	LYS460
D	GLY463
D	PHE464
D	ARG466
D	HOH2170

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1503

Chain	Residue
D	PHE281
D	TRP285
D	GLN448
D	PRO449
D	CYS450
D	HOH2177

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
C	PHE284-SER295
A	PHE284-SER295

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

Chain	Residue	Details
C	LEU256-PRO263
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)