1o04

Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+

Method: X-RAY DIFFRACTION D_max: 178.9 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Aldehyde dehydrogenase, mitochondrial precursor

Homo sapiens

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：Complete mature sequence (does not contain mitochondrial leader sequence). 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
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 18–517 Chain F； UniProt 18–517 Chain G； UniProt 18–517 Chain H； UniProt 18–517	Fragment：Complete mature sequence (does not contain mitochondrial leader sequence). 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

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 1O04	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 mutation/modification 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 mutation/modification 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 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 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 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).	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 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).	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 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).	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 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).	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 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).	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 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).	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 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).	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 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).	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 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).	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 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).	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
1O05 Apo form of human mitochondrial aldehyde dehydrogenase Deposited 2003-02-20	Different mutation/modification Different ligand/ion 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 mutation/modification Different ligand/ion 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 mutation/modification 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 mutation/modification 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 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）	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 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）	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 mutation/modification 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 mutation/modification 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
4FQF Crystal structure of a thionitrate intermediate of human aldehyde dehydrogenase-2 Deposited 2012-06-25	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：unp residues 18-517 Chain B 18–517（500 aa） Fragment：unp residues 18-517 Chain C 18–517（500 aa） Fragment：unp residues 18-517 Chain D 18–517（500 aa） Fragment：unp residues 18-517	Not recorded	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
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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 59 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 Author chain E； PDBConstruct 1–500； UniProt 18–517 Author chain F； PDBConstruct 1–500； UniProt 18–517 Author chain G； PDBConstruct 1–500； UniProt 18–517 Author chain H； 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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1o04
Deposition date deposition_date	2003-02-20
Structure title title	Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+
Keywords keywords	ALDH, NAD, NADH, isomerization, Oxidoreductase; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	61.98 Å
Radius of gyration Rg (electron density) rg_electron	62.45 Å
Forward intensity I(0) i0	2725640000.00
Molecular weight molecular_weight	439880.0 kDa
Excluded volume excluded_volume	549750 Å³
Envelope volume envelope_volume	704480 Å³
Hydration-shell volume shell_volume	94251 Å³
Envelope diameter envelope_diameter	197.6 Å
Shell Rg shell_rg	61.20 Å
Envelope Rg envelope_rg	61.45 Å
Shape Rg shape_rg	62.44 Å
Total Rg total_rg	62.48 Å
Total atoms total_atoms	30952
Residues n_residues	3952
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	178.9 Å
Rg (real space) rg_real	62.39 Å
Rg uncertainty (real space) rg_real_error	1.43 Å
I(0) (real space) i0_real	2.7260e+09
I(0) uncertainty (real space) i0_real_error	5.1550e+07
Rg (reciprocal space) rg_reciprocal	61.53 Å
I(0) (reciprocal space) i0_reciprocal	2721000000.0000
Solution quality estimate total_estimate	0.7861
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	50.1 Å
Skewness Skewness skewness	0.321
Kurtosis Kurtosis kurtosis	-0.946
Angular range angular_range	— – 0.1250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	193600000.0000
Real-space data points n_real_points	26
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.783; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.867; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Aldehyde dehydrogenase, mitochondrial precursor
Molecular weight formula_weight	54483.6 kDa
EC 编号 ec_number	1.2.1.3
Mutation mutation	C302S
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	36161

SAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCSCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
Molecular weight formula_weight	663.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 non-polymer

Description description	GUANIDINE
Molecular weight formula_weight	59.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 6 Entity 6 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	32

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	5025

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7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1o04a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

Domain ID domain_id	d1o04h_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.82 — ALDH-like
Superfamily Superfamily superfamily	c.82.1 — ALDH-like
Family Family family	c.82.1.1 — ALDH-like

CATH v4.4 (16 domains)

Domain ID domain_id	1o04A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04C01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04C02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04D01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04D02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04E01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04E02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04F01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04F02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04G01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04G02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

Domain ID domain_id	1o04H01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	605 — Aldehyde Dehydrogenase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 1

Domain ID domain_id	1o04H02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	309 — Aldehyde Dehydrogenase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Aldehyde Dehydrogenase; Chain A, domain 2

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8. Citations (1)

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Unit-cell length a length_a	141.211 Å
Unit-cell length b length_b	152.487 Å
Unit-cell length c length_c	177.200 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.420 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1466
R_work r_work	0.1453
R_free r_free	0.1712

fit	/app/data/saxs_computation/o0/1o04/1o04.fit
pddf	/app/data/pr_computation/o0/1o04/1o04.pr.out
profile	/app/data/saxs_computation/o0/1o04/1o04.dat