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8DR9

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005975biological_processcarbohydrate metabolic process
A0006066biological_processalcohol metabolic process
A0006068biological_processethanol catabolic process
A0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0018547molecular_functionnitroglycerin reductase activity
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
A0046185biological_processaldehyde catabolic process
A0051287molecular_functionNAD binding
A0070062cellular_componentextracellular exosome
A0106435molecular_functioncarboxylesterase activity
A1903179biological_processregulation of dopamine biosynthetic process
A1905627biological_processregulation of serotonin biosynthetic process
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005975biological_processcarbohydrate metabolic process
B0006066biological_processalcohol metabolic process
B0006068biological_processethanol catabolic process
B0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0018547molecular_functionnitroglycerin reductase activity
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0046185biological_processaldehyde catabolic process
B0051287molecular_functionNAD binding
B0070062cellular_componentextracellular exosome
B0106435molecular_functioncarboxylesterase activity
B1903179biological_processregulation of dopamine biosynthetic process
B1905627biological_processregulation of serotonin biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU267-PRO274

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU268
BGLU268

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER302
BSER302

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY245
BGLY245

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000
ChainResidueDetails
AASN169
BASN169

site_idSWS_FT_FI5
Number of Residues18
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47738
ChainResidueDetails
ALYS35
BLYS35
BLYS56
BLYS61
BLYS142
BLYS351
BLYS366
BLYS409
BLYS411
BLYS434
ALYS56
ALYS61
ALYS142
ALYS351
ALYS366
ALYS409
ALYS411
ALYS434

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 803
ChainResidueDetails
ALYS192electrostatic stabiliser
AGLU268electrostatic stabiliser, proton acceptor, proton donor
ASER302covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
AGLU399electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 803
ChainResidueDetails
BLYS192electrostatic stabiliser
BGLU268electrostatic stabiliser, proton acceptor, proton donor
BSER302covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
BGLU399electrostatic stabiliser

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PDB entries from 2024-07-17

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