Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6QAP

Structure of the human aldehyde dehydrogenase 9A1 in C2 space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006081	biological_process	aldehyde metabolic process
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	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
A	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
A	0036094	molecular_function	small molecule binding
A	0042429	biological_process	serotonin catabolic process
A	0045329	biological_process	carnitine biosynthetic process
A	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
A	0051289	biological_process	protein homotetramerization
A	0070062	cellular_component	extracellular exosome
A	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity
B	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006081	biological_process	aldehyde metabolic process
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	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
B	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
B	0036094	molecular_function	small molecule binding
B	0042429	biological_process	serotonin catabolic process
B	0045329	biological_process	carnitine biosynthetic process
B	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
B	0051289	biological_process	protein homotetramerization
B	0070062	cellular_component	extracellular exosome
B	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity
C	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006081	biological_process	aldehyde metabolic process
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	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
C	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
C	0036094	molecular_function	small molecule binding
C	0042429	biological_process	serotonin catabolic process
C	0045329	biological_process	carnitine biosynthetic process
C	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
C	0051289	biological_process	protein homotetramerization
C	0070062	cellular_component	extracellular exosome
C	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity
D	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006081	biological_process	aldehyde metabolic process
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	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
D	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
D	0036094	molecular_function	small molecule binding
D	0042429	biological_process	serotonin catabolic process
D	0045329	biological_process	carnitine biosynthetic process
D	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
D	0051289	biological_process	protein homotetramerization
D	0070062	cellular_component	extracellular exosome
D	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue EDO A 501

Chain	Residue
A	SER229

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

Chain	Residue
A	LYS227
A	VAL228

site_id	AC3
Number of Residues	8
Details	binding site for residue EDO A 503

Chain	Residue
A	THR44
A	GLN210
A	PRO11
A	LEU12
A	ASN13
A	GLU21
A	PRO22
A	PHE43

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 504

Chain	Residue
A	GLU118
A	TYR119
A	HOH610
D	CYS74
D	GLY122
D	HOH617

site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 505

Chain	Residue
A	GLY154
A	ALA155
A	PRO159
A	PHE179
A	PRO181
A	SER182
A	THR185
A	HOH603

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO B 501

Chain	Residue
B	GLU118
B	TYR119
B	GLY122
C	GLY122
C	PEG506

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO B 502

Chain	Residue
B	ARG467
B	ARG471
B	HOH636
C	ARG467

site_id	AC8
Number of Residues	1
Details	binding site for residue EDO B 503

Chain	Residue
B	SER229

site_id	AC9
Number of Residues	5
Details	binding site for residue PEG B 504

Chain	Residue
B	ASP24
B	ALA25
B	LYS49
C	THR28
C	GLU29

site_id	AD1
Number of Residues	1
Details	binding site for residue NA C 501

Chain	Residue
C	HOH677

site_id	AD2
Number of Residues	2
Details	binding site for residue NA C 502

Chain	Residue
C	GLN10
C	GLU194

site_id	AD3
Number of Residues	2
Details	binding site for residue NA C 503

Chain	Residue
C	SER9
C	GLN10

site_id	AD4
Number of Residues	1
Details	binding site for residue EDO C 504

Chain	Residue
C	SER9

site_id	AD5
Number of Residues	4
Details	binding site for residue PEG C 505

Chain	Residue
C	SER229
C	VAL472
C	THR473
C	TYR476

site_id	AD6
Number of Residues	7
Details	binding site for residue PEG C 506

Chain	Residue
B	MET71
B	CYS74
B	GLY122
B	EDO501
B	HOH610
C	GLN115
C	GLU118

site_id	AD7
Number of Residues	8
Details	binding site for residue PEG C 507

Chain	Residue
C	ILE153
C	GLY154
C	LYS180
C	SER182
C	PRO183
C	GLY212
C	ALA213
C	HOH621

site_id	AD8
Number of Residues	8
Details	binding site for residue NA D 501

Chain	Residue
D	TYR14
D	ARG15
D	GLY16
D	GLY17
D	GLY204
D	PHE206
D	ASN207
D	EDO507

site_id	AD9
Number of Residues	2
Details	binding site for residue NA D 502

Chain	Residue
D	GLU118
D	EDO506

site_id	AE1
Number of Residues	4
Details	binding site for residue NA D 503

Chain	Residue
D	ALA155
D	PRO181
D	SER182
D	THR185

site_id	AE2
Number of Residues	2
Details	binding site for residue NA D 504

Chain	Residue
D	SER9
D	GLN10

site_id	AE3
Number of Residues	2
Details	binding site for residue NA D 505

Chain	Residue
D	GLN10
D	GLU194

site_id	AE4
Number of Residues	5
Details	binding site for residue EDO D 506

Chain	Residue
A	GLY122
D	GLU118
D	TYR119
D	GLY122
D	NA502

site_id	AE5
Number of Residues	10
Details	binding site for residue EDO D 507

Chain	Residue
D	GLY17
D	SER197
D	VAL201
D	PRO202
D	PRO203
D	GLY204
D	LEU205
D	PHE206
D	NA501
D	HOH603

site_id	AE6
Number of Residues	7
Details	binding site for residue EDO D 508

Chain	Residue
D	ASN13
D	GLU21
D	PRO22
D	PHE43
D	THR44
D	GLN210
D	LEU12

site_id	AE7
Number of Residues	2
Details	binding site for residue EDO D 509

Chain	Residue
D	GLU198
D	GLY200

site_id	AE8
Number of Residues	3
Details	binding site for residue EDO D 510

Chain	Residue
D	PHE104
D	ARG107
D	LEU108

site_id	AE9
Number of Residues	4
Details	binding site for residue EDO D 511

Chain	Residue
C	GLU468
D	ALA128
D	GLY129
D	ARG144

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE281-THR292

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

Chain	Residue	Details
A	LEU253-PRO260

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P56533","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Gottlieb E."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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