8DR9

Crystal structure of human ALDH2 in complex with NAD+ and PEG MME 550

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001758	molecular_function	retinal dehydrogenase (NAD+) activity
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0004777	molecular_function	succinate-semialdehyde dehydrogenase (NAD+) activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006068	biological_process	ethanol catabolic process
A	0008957	molecular_function	phenylacetaldehyde dehydrogenase (NAD+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
A	0018937	biological_process	nitroglycerin metabolic process
A	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
A	0042420	biological_process	dopamine catabolic process
A	0046185	biological_process	aldehyde catabolic process
A	0046857	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
A	0051287	molecular_function	NAD binding
A	0052814	molecular_function	medium-chain fatty aldehyde dehydrogenase (NAD+) activity
A	0070062	cellular_component	extracellular exosome
A	0106435	molecular_function	carboxylesterase activity
A	0110095	biological_process	cellular detoxification of aldehyde
A	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity
B	0001758	molecular_function	retinal dehydrogenase (NAD+) activity
B	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
B	0004777	molecular_function	succinate-semialdehyde dehydrogenase (NAD+) activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006068	biological_process	ethanol catabolic process
B	0008957	molecular_function	phenylacetaldehyde dehydrogenase (NAD+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0018467	molecular_function	formaldehyde dehydrogenase (NAD+) activity
B	0018937	biological_process	nitroglycerin metabolic process
B	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
B	0042420	biological_process	dopamine catabolic process
B	0046185	biological_process	aldehyde catabolic process
B	0046857	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
B	0052814	molecular_function	medium-chain fatty aldehyde dehydrogenase (NAD+) activity
B	0070062	cellular_component	extracellular exosome
B	0106435	molecular_function	carboxylesterase activity
B	0110095	biological_process	cellular detoxification of aldehyde
B	0140087	molecular_function	acetaldehyde dehydrogenase (NAD+) activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU267-PRO274

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19506075","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19506075","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12795606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O02","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12795606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NZW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22988236","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FQF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FR8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12795606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O02","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12795606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O01","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"22988236","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	18
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P47738","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 803

Chain	Residue	Details
A	LYS192	electrostatic stabiliser
A	GLU268	electrostatic stabiliser, proton acceptor, proton donor
A	SER302	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLU399	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 803

Chain	Residue	Details
B	LYS192	electrostatic stabiliser
B	GLU268	electrostatic stabiliser, proton acceptor, proton donor
B	SER302	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	GLU399	electrostatic stabiliser

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