Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4X0T

Structure ALDH7A1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0004043	molecular_function	L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006081	biological_process	aldehyde metabolic process
A	0006554	biological_process	lysine catabolic process
A	0007605	biological_process	sensory perception of sound
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	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0019477	biological_process	L-lysine catabolic process
A	0042426	biological_process	choline catabolic process
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
B	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
B	0004043	molecular_function	L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006081	biological_process	aldehyde metabolic process
B	0006554	biological_process	lysine catabolic process
B	0007605	biological_process	sensory perception of sound
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	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0019477	biological_process	L-lysine catabolic process
B	0042426	biological_process	choline catabolic process
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
C	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
C	0004043	molecular_function	L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0006081	biological_process	aldehyde metabolic process
C	0006554	biological_process	lysine catabolic process
C	0007605	biological_process	sensory perception of sound
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	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0019477	biological_process	L-lysine catabolic process
C	0042426	biological_process	choline catabolic process
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
D	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
D	0004043	molecular_function	L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006081	biological_process	aldehyde metabolic process
D	0006554	biological_process	lysine catabolic process
D	0007605	biological_process	sensory perception of sound
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	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0019477	biological_process	L-lysine catabolic process
D	0042426	biological_process	choline catabolic process
D	0042802	molecular_function	identical protein binding
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue NAD A 601

Chain	Residue
A	ILE163
A	ALA227
A	GLY230
A	THR231
A	PHE244
A	THR245
A	GLY246
A	SER247
A	VAL250
A	GLU268
A	LEU269
A	THR164
A	GLY270
A	GLU399
A	PHE401
A	PHE468
A	3W9602
A	HOH706
A	HOH752
A	HOH773
B	HOH704
A	ALA165
A	PHE166
A	ASN167
A	LYS190
A	GLY191
A	ALA192
A	PRO193

site_id	AC2
Number of Residues	6
Details	binding site for residue 3W9 A 602

Chain	Residue
A	ASN167
A	PHE168
A	ALA171
A	TRP175
A	PHE468
A	NAD601

site_id	AC3
Number of Residues	29
Details	binding site for residue NAD B 601

Chain	Residue
B	ILE163
B	THR164
B	ALA165
B	PHE166
B	ASN167
B	LYS190
B	GLY191
B	ALA192
B	PRO193
B	ALA227
B	GLY230
B	THR231
B	PHE244
B	THR245
B	GLY246
B	SER247
B	VAL250
B	VAL254
B	GLU268
B	LEU269
B	GLY270
B	GLU399
B	PHE401
B	PHE468
B	3W9602
B	HOH713
B	HOH752
B	HOH767
B	HOH768

site_id	AC4
Number of Residues	8
Details	binding site for residue 3W9 B 602

Chain	Residue
B	ASN167
B	PHE168
B	ALA171
B	TRP175
B	ARG301
B	PHE468
B	GLU479
B	NAD601

site_id	AC5
Number of Residues	28
Details	binding site for residue NAD C 601

Chain	Residue
C	ILE163
C	THR164
C	ALA165
C	PHE166
C	ASN167
C	LYS190
C	GLY191
C	ALA192
C	PRO193
C	ALA227
C	GLY230
C	THR231
C	PHE244
C	THR245
C	GLY246
C	SER247
C	VAL250
C	GLU268
C	LEU269
C	GLY270
C	GLU399
C	PHE401
C	PHE468
C	3W9602
C	HOH709
C	HOH747
C	HOH754
C	HOH775

site_id	AC6
Number of Residues	8
Details	binding site for residue 3W9 C 602

Chain	Residue
C	ASN167
C	PHE168
C	ALA171
C	TRP175
C	ARG301
C	PHE468
C	GLU479
C	NAD601

site_id	AC7
Number of Residues	26
Details	binding site for residue NAD D 601

Chain	Residue
D	ILE163
D	THR164
D	ALA165
D	PHE166
D	ASN167
D	LYS190
D	ALA192
D	PRO193
D	ALA227
D	GLY230
D	THR231
D	PHE244
D	THR245
D	GLY246
D	SER247
D	VAL250
D	VAL254
D	GLU268
D	LEU269
D	GLY270
D	GLU399
D	PHE401
D	3W9602
D	HOH702
D	HOH728
D	HOH741

site_id	AC8
Number of Residues	8
Details	binding site for residue 3W9 D 602

Chain	Residue
D	ASN167
D	PHE168
D	ALA171
D	TRP175
D	ARG301
D	PHE468
D	GLU479
D	NAD601

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU267-ALA274

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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20207735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J6L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X0T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZUK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZVY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20207735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J6L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X0T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"4ZUL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DBF1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBF1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBF1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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