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4fqf

Crystal structure of a thionitrate intermediate of human aldehyde dehydrogenase-2

Method: X-RAY DIFFRACTION Dmax: 110.8 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Aldehyde dehydrogenase, mitochondrial

Homo sapiens

UniProt P05091

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 18–517 Chain B； UniProt 18–517 Chain C； UniProt 18–517 Chain D； UniProt 18–517 Fragment：unp residues 18-517 2NO NITROGEN DIOXIDE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 MG MAGNESIUM ION × 4 URE UREA × 6 NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；100 mM bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (Bis-TRIS), 25% PEG 3350, 60 mM urea; 13.3 mM magnesium chloride, 8.9 mM tris(2-carboxyethyl)phosphine (TCEP), 4.4 mM NAD+, 45.8 mM glucose, crystals have been soaked with glyceryl trinitrate (GTN), pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.28 Å R-free 0.209

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 4FQF Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CW3 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Deposited 1999-08-25 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain B 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain C 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain D 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Not recorded MN MANGANESE (II) ION × 4 MG MAGNESIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；100 MM ACES, PH 6.4, 100 MM GUANIDINE-HCL, 2 MM NAD+, 4 MM DTT, 16% PEG 6000, 8 MG/ML ENZYME SOAKED WITH 8 MM MNCL2 FOR 2 DAYS, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.58 Å R-free 0.242
1CW3 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Deposited 1999-08-25 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain F 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain G 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Chain H 24–517（494 aa） Fragment：COMPLETE MATURE SEQUENCE (DOES NOT INCLUDE MITOCHONDRIAL LEADER SEQUENCE)
Not recorded MN MANGANESE (II) ION × 4 MG MAGNESIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；100 MM ACES, PH 6.4, 100 MM GUANIDINE-HCL, 2 MM NAD+, 4 MM DTT, 16% PEG 6000, 8 MG/ML ENZYME SOAKED WITH 8 MM MNCL2 FOR 2 DAYS, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.58 Å R-free 0.242
1NZW Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NADH and Mg2+ Deposited 2003-02-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Mutation：C302S Mutation：C302S Mutation：C302S Mutation：C302S NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NADH at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.65 Å R-free 0.252
1NZW Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NADH and Mg2+ Deposited 2003-02-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Mutation：C302S Mutation：C302S Mutation：C302S Mutation：C302S NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NADH at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.65 Å R-free 0.252
1NZX Human mitochondrial aldehyde dehydrogenase complexed with NAD+ in the presence of low Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked at decreasing concentrations of Mg2+ and then with NAD+ and 0 Mg2+ prior to data collection. , pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.45 Å R-free 0.245
1NZX Human mitochondrial aldehyde dehydrogenase complexed with NAD+ in the presence of low Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked at decreasing concentrations of Mg2+ and then with NAD+ and 0 Mg2+ prior to data collection. , pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.45 Å R-free 0.245
1NZZ Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of low Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked at increasing pH and decreasing concentrations of Mg2+ and then with NADH and 0.2 mM Mg2+ at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.45 Å R-free 0.248
1NZZ Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of low Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked at increasing pH and decreasing concentrations of Mg2+ and then with NADH and 0.2 mM Mg2+ at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.45 Å R-free 0.248
1O00 Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ showing dual NAD(H) conformations Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NAD+ at pH 6.4 prior to data collection., VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.232
1O00 Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ showing dual NAD(H) conformations Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NAD+ at pH 6.4 prior to data collection., VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.232
1O01 Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(H) and Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 CRD (2E)-BUT-2-ENAL × 3 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT, NAD+. Crystal soaked with crotonaldehyde prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.15 Å R-free 0.206
1O01 Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(H) and Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 CRD (2E)-BUT-2-ENAL × 3 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT, NAD+. Crystal soaked with crotonaldehyde prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.15 Å R-free 0.206
1O02 Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 8 EDO 1,2-ETHANEDIOL × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NADH at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.90 Å R-free 0.213
1O02 Human mitochondrial aldehyde dehydrogenase complexed with NADH in the presence of Mg2+ Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 8 EDO 1,2-ETHANEDIOL × 4 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT. Crystal soaked with NADH at pH 7.0 prior to data collection., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.90 Å R-free 0.213
1O04 Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ Deposited 2003-02-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Mutation：C302S Mutation：C302S Mutation：C302S Mutation：C302S NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 GAI GUANIDINE × 9 EDO 1,2-ETHANEDIOL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.42 Å R-free 0.171
1O04 Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+ Deposited 2003-02-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Mutation：C302S Mutation：C302S Mutation：C302S Mutation：C302S NA SODIUM ION × 4 MG MAGNESIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 GAI GUANIDINE × 9 EDO 1,2-ETHANEDIOL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.42 Å R-free 0.171
1O05 Apo form of human mitochondrial aldehyde dehydrogenase Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain B 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain C 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain D 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.25 Å R-free 0.216
1O05 Apo form of human mitochondrial aldehyde dehydrogenase Deposited 2003-02-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain F 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain G 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Chain H 18–517（500 aa） Fragment：Complete mature sequence (does not contain mitochondrial leader sequence).
Not recorded NA SODIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；ACES, PEG 6000, Guanidine HCl, MgCl2, DTT., pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.25 Å R-free 0.216
1ZUM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, Apo Form Deposited 2005-05-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 4 GAI GUANIDINE × 1 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), magnesium chloride, Guanidine HCl, PEG 6000, DTT, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.10 Å R-free 0.238
1ZUM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, Apo Form Deposited 2005-05-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 4 GAI GUANIDINE × 5 EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), magnesium chloride, Guanidine HCl, PEG 6000, DTT, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.10 Å R-free 0.238
1ZUM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, Apo Form Deposited 2005-05-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 18–517（500 aa）
Chain J 18–517（500 aa）
Chain K 18–517（500 aa）
Chain L 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 4 GAI GUANIDINE × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.6；293 K；ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), magnesium chloride, Guanidine HCl, PEG 6000, DTT, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.10 Å R-free 0.238
2ONM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with NAD+ Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 2 EDO 1,2-ETHANEDIOL × 8 GAI GUANIDINE × 2 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 15% w/v PEG 6000, 8mM DTT, pH 6.8, VAPOR DIFFUSION, temperature 293K
Resolution 2.50 Å R-free 0.271
2ONM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with NAD+ Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 12 GAI GUANIDINE × 5 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 15% w/v PEG 6000, 8mM DTT, pH 6.8, VAPOR DIFFUSION, temperature 293K
Resolution 2.50 Å R-free 0.271
2ONM Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with NAD+ Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 18–517（500 aa）
Chain J 18–517（500 aa）
Chain K 18–517（500 aa）
Chain L 18–517（500 aa）
Mutation：E487K Mutation：E487K Mutation：E487K Mutation：E487K NA SODIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 4 EDO 1,2-ETHANEDIOL × 5 GAI GUANIDINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sulfonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 15% w/v PEG 6000, 8mM DTT, pH 6.8, VAPOR DIFFUSION, temperature 293K
Resolution 2.50 Å R-free 0.271
2ONN Arg475Gln Mutant of Human Mitochondrial Aldehyde Dehydrogenase, Apo form Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 16% w/v PEG 6000, 4 mM DTT, pH 6.6, vapor diffusion, temperature 293K
Resolution 2.75 Å R-free 0.268
2ONN Arg475Gln Mutant of Human Mitochondrial Aldehyde Dehydrogenase, Apo form Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 16% w/v PEG 6000, 4 mM DTT, pH 6.6, vapor diffusion, temperature 293K
Resolution 2.75 Å R-free 0.268
2ONO Arg475Gln Mutant of Mitochondrial Aldehyde Dehydrogenase, apo form, pseudo-merohedrally twinned Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 5 mM MgCl2, 100 mM Guanidine HCl, 18% w/v PEG 6000, 6 mM DTT, pH 6.6, vapor diffusion, temperature 293K, pH 6.60
Resolution 2.15 Å R-free 0.314
2ONO Arg475Gln Mutant of Mitochondrial Aldehyde Dehydrogenase, apo form, pseudo-merohedrally twinned Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 5 mM MgCl2, 100 mM Guanidine HCl, 18% w/v PEG 6000, 6 mM DTT, pH 6.6, vapor diffusion, temperature 293K, pH 6.60
Resolution 2.15 Å R-free 0.314
2ONP Arg475Gln Mutant of Human Mitochondrial Aldehyde Dehydrogenase, complexed with NAD+ Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q MG MAGNESIUM ION × 4 NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 EDO 1,2-ETHANEDIOL × 19 GAI GUANIDINE × 15 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 16% w/v PEG 6000, 8 mM DTT, pH 6.6, vapor diffusion, temperature 293K
Resolution 2.00 Å R-free 0.240
2ONP Arg475Gln Mutant of Human Mitochondrial Aldehyde Dehydrogenase, complexed with NAD+ Deposited 2007-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：R475Q Mutation：R475Q Mutation：R475Q Mutation：R475Q MG MAGNESIUM ION × 4 NA SODIUM ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 EDO 1,2-ETHANEDIOL × 20 GAI GUANIDINE × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.6；293 K；100 mM ACES (N-[2-Acetamido]-2-aminoethane sufonic acid), 10mM MgCl2, 100 mM Guanidine HCl, 16% w/v PEG 6000, 8 mM DTT, pH 6.6, vapor diffusion, temperature 293K
Resolution 2.00 Å R-free 0.240
2VLE The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase Deposited 2008-01-13 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 24–517（494 aa） Fragment：RESIDUES 24-517
Chain B 24–517（494 aa） Fragment：RESIDUES 24-517
Chain C 24–517（494 aa） Fragment：RESIDUES 24-517
Chain D 24–517（494 aa） Fragment：RESIDUES 24-517
Not recorded DZN DAIDZIN × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；100 MM MES PH 6.5, 100 MM GUANIDINE-HCL, 3 MM DITHIOTHREITOL, 5% DMSO (V/V), 10% PEG 6000 (W/V) AND 2MM DAIDZIN
Resolution 2.40 Å R-free 0.249
2VLE The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase Deposited 2008-01-13 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 24–517（494 aa） Fragment：RESIDUES 24-517
Chain F 24–517（494 aa） Fragment：RESIDUES 24-517
Chain G 24–517（494 aa） Fragment：RESIDUES 24-517
Chain H 24–517（494 aa） Fragment：RESIDUES 24-517
Not recorded DZN DAIDZIN × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；100 MM MES PH 6.5, 100 MM GUANIDINE-HCL, 3 MM DITHIOTHREITOL, 5% DMSO (V/V), 10% PEG 6000 (W/V) AND 2MM DAIDZIN
Resolution 2.40 Å R-free 0.249
3INJ Human Mitochondrial Aldehyde Dehydrogenase complexed with agonist Alda-1 Deposited 2009-08-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Not recorded NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 9 GAI GUANIDINE × 4 BXB N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 8MM DTT, pH 6.4, VAPOR DIFFUSION, temperature 292K
Resolution 1.69 Å R-free 0.200
3INJ Human Mitochondrial Aldehyde Dehydrogenase complexed with agonist Alda-1 Deposited 2009-08-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Not recorded NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 7 GAI GUANIDINE × 5 BXB N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 8MM DTT, pH 6.4, VAPOR DIFFUSION, temperature 292K
Resolution 1.69 Å R-free 0.200
3INL Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with agonist Alda-1 Deposited 2009-08-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：E487K, C302S Mutation：E487K, C302S Mutation：E487K, C302S Mutation：E487K, C302S NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 15 BXB N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 8MM DTT, pH 6.4, VAPOR DIFFUSION, temperature 292K
Resolution 1.86 Å R-free 0.168
3INL Human Mitochondrial Aldehyde Dehydrogenase Asian Variant, ALDH2*2, complexed with agonist Alda-1 Deposited 2009-08-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：E487K, C302S Mutation：E487K, C302S Mutation：E487K, C302S Mutation：E487K, C302S NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 16 BXB N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 8MM DTT, pH 6.4, VAPOR DIFFUSION, temperature 292K
Resolution 1.86 Å R-free 0.168
3N80 Human mitochondrial aldehyde dehydrogenase, apo form Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain C 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GAI GUANIDINE × 10 EDO 1,2-ETHANEDIOL × 18 NA SODIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.50 Å R-free 0.175
3N80 Human mitochondrial aldehyde dehydrogenase, apo form Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain G 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GAI GUANIDINE × 11 EDO 1,2-ETHANEDIOL × 18 NA SODIUM ION × 4 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.50 Å R-free 0.175
3N81 T244A mutant of Human mitochondrial aldehyde dehydrogenase, apo form Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain C 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A NA SODIUM ION × 4 GAI GUANIDINE × 10 EDO 1,2-ETHANEDIOL × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.70 Å R-free 0.217
3N81 T244A mutant of Human mitochondrial aldehyde dehydrogenase, apo form Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain G 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A NA SODIUM ION × 4 GAI GUANIDINE × 11 EDO 1,2-ETHANEDIOL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.70 Å R-free 0.217
3N82 T244A mutant of Human mitochondrial aldehyde dehydrogenase, NADH complex Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain C 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 6 EDO 1,2-ETHANEDIOL × 11 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.25 Å R-free 0.219
3N82 T244A mutant of Human mitochondrial aldehyde dehydrogenase, NADH complex Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain G 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A MG MAGNESIUM ION × 4 NA SODIUM ION × 4 GAI GUANIDINE × 7 EDO 1,2-ETHANEDIOL × 13 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.25 Å R-free 0.219
3N83 T244A mutant of human mitochondrial aldehyde dehydrogenase, NAD complex Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain C 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A NA SODIUM ION × 4 GAI GUANIDINE × 7 EDO 1,2-ETHANEDIOL × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.90 Å R-free 0.232
3N83 T244A mutant of human mitochondrial aldehyde dehydrogenase, NAD complex Deposited 2010-05-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain G 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, residues 18-517
Mutation：T244A Mutation：T244A Mutation：T244A Mutation：T244A NA SODIUM ION × 4 GAI GUANIDINE × 9 EDO 1,2-ETHANEDIOL × 12 ADP ADENOSINE-5'-DIPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE HCL, 16-17% W/V PEG 6000, pH 6.4, vapor diffusion, temperature 292K
Resolution 1.90 Å R-free 0.232
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 2 GAI GUANIDINE × 4 EDO 1,2-ETHANEDIOL × 3 I3E 1-(4-ethylphenyl)propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 2 GAI GUANIDINE × 5 EDO 1,2-ETHANEDIOL × 6 I3E 1-(4-ethylphenyl)propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 2 GAI GUANIDINE × 5 EDO 1,2-ETHANEDIOL × 8 I3E 1-(4-ethylphenyl)propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain G 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 2 GAI GUANIDINE × 4 EDO 1,2-ETHANEDIOL × 4 I3E 1-(4-ethylphenyl)propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain B 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain C 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain D 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 4 GAI GUANIDINE × 9 EDO 1,2-ETHANEDIOL × 9 I3E 1-(4-ethylphenyl)propan-1-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
3SZ9 Crystal structure of human ALDH2 modified with the beta-elimination product of Aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one Deposited 2011-07-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain F 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain G 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Chain H 18–517（500 aa） Fragment：Mature sequence, UNP residues 18-517
Not recorded NA SODIUM ION × 4 GAI GUANIDINE × 9 EDO 1,2-ETHANEDIOL × 12 I3E 1-(4-ethylphenyl)propan-1-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.4；292 K；100 MM ACES (N-[2-ACETAMIDO]-2-AMINOETHANE SULFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16-17% W/V PEG 6000, 4MM DTT, pH 6.4, vapor diffusion, temperature 292K
Resolution 2.10 Å R-free 0.226
4FR8 Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin Deposited 2012-06-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Chain C 18–517（500 aa）
Chain D 18–517（500 aa）
Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S TNG propane-1,2,3-triyl trinitrate × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 3 MG MAGNESIUM ION × 4 URE UREA × 5 NA SODIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；100 mM bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (Bis-TRIS), 25% PEG 3350, 60 mM urea; 6.9 mM magnesium chloride, 4.6 mM tris(2-carboxyethyl)phosphine (TCEP), 2.3 mM NAD+, 47.6 mM glucose, crystals have been soaked with glyceryl trinitrate (GTN), pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.167
4FR8 Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin Deposited 2012-06-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 18–517（500 aa）
Chain F 18–517（500 aa）
Chain G 18–517（500 aa）
Chain H 18–517（500 aa）
Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S Mutation：E268Q, C301S, C303S NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 MG MAGNESIUM ION × 4 URE UREA × 1 NA SODIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；293 K；100 mM bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (Bis-TRIS), 25% PEG 3350, 60 mM urea; 6.9 mM magnesium chloride, 4.6 mM tris(2-carboxyethyl)phosphine (TCEP), 2.3 mM NAD+, 47.6 mM glucose, crystals have been soaked with glyceryl trinitrate (GTN), pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.167
4KWF Crystal Structure Analysis of ALDH2+ALDiB33 Deposited 2013-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 24–517（494 aa） Fragment：UNP residues 24-517
Chain B 24–517（494 aa） Fragment：UNP residues 24-517
Chain C 24–517（494 aa） Fragment：UNP residues 24-517
Chain D 24–517（494 aa） Fragment：UNP residues 24-517
Not recorded 3AK 1-benzyl-1H-indole-2,3-dione × 2 NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 4 GAI GUANIDINE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions sitting drop；pH 6.4；300 K；100 mM ACES, 100 mm guanidine-HCl, 10 mm MgCl2, and 14-19% PEG 6000, pH 6.4, sitting drop, temperature 300K
Resolution 2.31 Å R-free 0.296
4KWF Crystal Structure Analysis of ALDH2+ALDiB33 Deposited 2013-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 24–517（494 aa） Fragment：UNP residues 24-517
Chain F 24–517（494 aa） Fragment：UNP residues 24-517
Chain G 24–517（494 aa） Fragment：UNP residues 24-517
Chain H 24–517（494 aa） Fragment：UNP residues 24-517
Not recorded 3AK 1-benzyl-1H-indole-2,3-dione × 2 NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 4 GAI GUANIDINE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions sitting drop；pH 6.4；300 K；100 mM ACES, 100 mm guanidine-HCl, 10 mm MgCl2, and 14-19% PEG 6000, pH 6.4, sitting drop, temperature 300K
Resolution 2.31 Å R-free 0.296
4KWG Crystal Structure Analysis of ALDH2+ALDiB13 Deposited 2013-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 24–517（494 aa） Fragment：UNP residues 24-517
Chain B 24–517（494 aa） Fragment：UNP residues 24-517
Chain C 24–517（494 aa） Fragment：UNP residues 24-517
Chain D 24–517（494 aa） Fragment：UNP residues 24-517
Not recorded 2AK 7-bromo-5-methyl-1H-indole-2,3-dione × 1 NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 4 GAI GUANIDINE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions sitting drop；pH 6.4；300 K；100 mM ACES, 100 mm guanidine-HCl, 10 mm MgCl2, and 14-19% PEG 6000, pH 6.4, sitting drop, temperature 300K
Resolution 2.10 Å R-free 0.229
4KWG Crystal Structure Analysis of ALDH2+ALDiB13 Deposited 2013-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 24–517（494 aa） Fragment：UNP residues 24-517
Chain F 24–517（494 aa） Fragment：UNP residues 24-517
Chain G 24–517（494 aa） Fragment：UNP residues 24-517
Chain H 24–517（494 aa） Fragment：UNP residues 24-517
Not recorded 2AK 7-bromo-5-methyl-1H-indole-2,3-dione × 1 NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 4 GAI GUANIDINE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions sitting drop；pH 6.4；300 K；100 mM ACES, 100 mm guanidine-HCl, 10 mm MgCl2, and 14-19% PEG 6000, pH 6.4, sitting drop, temperature 300K
Resolution 2.10 Å R-free 0.229
5L13 Structure of ALDH2 in complex with 2P3 Deposited 2016-07-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–517（517 aa）
Chain B 1–517（517 aa）
Chain C 1–517（517 aa）
Chain D 1–517（517 aa）
Not recorded NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 5 GAI GUANIDINE × 8 6ZE 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；300 K；100 mM ACES, 100 mM guanidine-HCl, 10 mM MgCl2, 4 mM dithiothreitol, 18% PEG6000
Resolution 2.40 Å R-free 0.206
5L13 Structure of ALDH2 in complex with 2P3 Deposited 2016-07-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–517（517 aa）
Chain F 1–517（517 aa）
Chain G 1–517（517 aa）
Chain H 1–517（517 aa）
Not recorded NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 7 GAI GUANIDINE × 8 6ZE 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.4；300 K；100 mM ACES, 100 mM guanidine-HCl, 10 mM MgCl2, 4 mM dithiothreitol, 18% PEG6000
Resolution 2.40 Å R-free 0.206
8DR9 Crystal structure of human ALDH2 in complex with NAD+ and PEG MME 550 Deposited 2022-07-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 18–517（500 aa）
Chain B 18–517（500 aa）
Mutation：C302S Mutation：C302S CIT CITRIC ACID × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 NA SODIUM ION × 4 1PE PENTAETHYLENE GLYCOL × 18 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；protein conditions: 8 mg/ml recombinant ALDH2 in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, 1 mM DTT, supplemented with 2-4% v/v DMSO well conditions: 100 mM sodium citrate, pH 5.0-5.6, 22-26% w/v PEG MME 550 550 hanging drops were set with a 1.5:1 protein:well ratio
Resolution 1.50 Å R-free 0.157
8SHS human liver mitochondrial Aldehyde dehydrogenase ALDH2 Deposited 2023-04-14 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–517（517 aa）
Chain B 1–517（517 aa）
Chain C 1–517（517 aa）
Chain D 1–517（517 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.66 Å

28 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ALDH2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–500； UniProt 18–517 Author chain B； PDBConstruct 1–500； UniProt 18–517 Author chain C； PDBConstruct 1–500； UniProt 18–517 Author chain D； PDBConstruct 1–500； UniProt 18–517

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4fqf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4fqf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4fqf
Deposition date deposition_date2012-06-25
Structure title titleCrystal structure of a thionitrate intermediate of human aldehyde dehydrogenase-2
Keywords keywordsRossmann Fold, oxidoreductase, aldehydes, esters, organic nitrates, NAD, oxidoreductase-intermediate complex; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier36.65 Å
Radius of gyration Rg (electron density) rg_electron35.94 Å
Forward intensity I(0) i0716254000.00
Molecular weight molecular_weight218260.0 kDa
Excluded volume excluded_volume272610 ų
Envelope volume envelope_volume319080 ų
Hydration-shell volume shell_volume69606 ų
Envelope diameter envelope_diameter114.2 Å
Shell Rg shell_rg45.32 Å
Envelope Rg envelope_rg35.98 Å
Shape Rg shape_rg35.92 Å
Total Rg total_rg36.51 Å
Total atoms total_atoms15358
Residues n_residues1967
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax110.8 Å
Rg (real space) rg_real36.38 Å
Rg uncertainty (real space) rg_real_error0.67 Å
I(0) (real space) i0_real7.1630e+08
I(0) uncertainty (real space) i0_real_error1.0550e+07
Rg (reciprocal space) rg_reciprocal36.55 Å
I(0) (reciprocal space) i0_reciprocal716400000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary— Å
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.2150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha172400000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.929
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4fqfa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.82 — ALDH-like
Superfamily Superfamily superfamilyc.82.1 — ALDH-like
Family Family familyc.82.1.1 — ALDH-like
Domain ID domain_idd4fqfb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.82 — ALDH-like
Superfamily Superfamily superfamilyc.82.1 — ALDH-like
Family Family familyc.82.1.1 — ALDH-like
Domain ID domain_idd4fqfc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.82 — ALDH-like
Superfamily Superfamily superfamilyc.82.1 — ALDH-like
Family Family familyc.82.1.1 — ALDH-like
Domain ID domain_idd4fqfd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.82 — ALDH-like
Superfamily Superfamily superfamilyc.82.1 — ALDH-like
Family Family familyc.82.1.1 — ALDH-like

CATH v4.4 (8 domains)

Domain ID domain_id4fqfA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 1
Domain ID domain_id4fqfA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 2
Domain ID domain_id4fqfB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 1
Domain ID domain_id4fqfB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 2
Domain ID domain_id4fqfC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 1
Domain ID domain_id4fqfC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 2
Domain ID domain_id4fqfD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 1
Domain ID domain_id4fqfD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Aldehyde Dehydrogenase; Chain A, domain 2
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8. Citations (1)

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9. Files and Curves (10)