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- PDB-3n82: T244A mutant of Human mitochondrial aldehyde dehydrogenase, NADH ... -

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Basic information

Entry
Database: PDB / ID: 3n82
TitleT244A mutant of Human mitochondrial aldehyde dehydrogenase, NADH complex
ComponentsAldehyde dehydrogenase, mitochondrial
KeywordsOXIDOREDUCTASE / ALDH / Rossmann fold
Function / homology
Function and homology information


Metabolism of serotonin / nitroglycerin reductase activity / regulation of dopamine biosynthetic process / regulation of serotonin biosynthetic process / phenylacetaldehyde dehydrogenase activity / aldehyde catabolic process / alcohol metabolic process / aldehyde dehydrogenase [NAD(P)+] activity / ethanol catabolic process / Ethanol oxidation ...Metabolism of serotonin / nitroglycerin reductase activity / regulation of dopamine biosynthetic process / regulation of serotonin biosynthetic process / phenylacetaldehyde dehydrogenase activity / aldehyde catabolic process / alcohol metabolic process / aldehyde dehydrogenase [NAD(P)+] activity / ethanol catabolic process / Ethanol oxidation / aldehyde dehydrogenase (NAD+) / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity / aldehyde dehydrogenase (NAD+) activity / carboxylic ester hydrolase activity / NAD binding / electron transfer activity / mitochondrial matrix / carbohydrate metabolic process / mitochondrion / extracellular exosome
Similarity search - Function
Aldehyde Dehydrogenase; Chain A, domain 2 / Aldehyde Dehydrogenase; Chain A, domain 2 / Aldehyde Dehydrogenase; Chain A, domain 1 / Aldehyde Dehydrogenase; Chain A, domain 1 / Aldehyde dehydrogenase, cysteine active site / Aldehyde dehydrogenases cysteine active site. / Aldehyde dehydrogenase, glutamic acid active site / Aldehyde dehydrogenases glutamic acid active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family ...Aldehyde Dehydrogenase; Chain A, domain 2 / Aldehyde Dehydrogenase; Chain A, domain 2 / Aldehyde Dehydrogenase; Chain A, domain 1 / Aldehyde Dehydrogenase; Chain A, domain 1 / Aldehyde dehydrogenase, cysteine active site / Aldehyde dehydrogenases cysteine active site. / Aldehyde dehydrogenase, glutamic acid active site / Aldehyde dehydrogenases glutamic acid active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANIDINE / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Aldehyde dehydrogenase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Direct Refinement / Resolution: 2.25 Å
AuthorsGonzalez-Segura, L. / Hurley, T.D.
Citation
Journal: To be published
Title: Conformational Selection During Catalysis: The role of Threonine 244 in ALDH2
Authors: Ho, K.-K. / Gonzalez-Segura, L. / Perez-Miller, S. / Weiner, H. / Hurley, T.D.
#1: Journal: Biochemistry / Year: 2006
Title: Selective Alteration of the Rate-Limiting Step in Cytosolic Aldehyde Dehydrogenase through Random Mutagenesis
Authors: Ho, K.-K. / Hurley, T.D. / Weiner, H.
#2: Journal: J. Biol. Chem. / Year: 2007
Title: Structural and Functional Consequences of Coenzyme Binding to the Inactive Asian Variant of Mitochondrial Aldehyde Dehydrogenase (ROLES OF RESIDUES 475 AND 487)
Authors: Larson, H.N. / Zhou, J. / Chen, Z. / Stamler, J.S. / Weiner, H. / Hurley, T.D.
History
DepositionMay 27, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 13, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software
Revision 1.3Jan 31, 2018Group: Database references / Category: citation_author / Item: _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aldehyde dehydrogenase, mitochondrial
B: Aldehyde dehydrogenase, mitochondrial
C: Aldehyde dehydrogenase, mitochondrial
D: Aldehyde dehydrogenase, mitochondrial
E: Aldehyde dehydrogenase, mitochondrial
F: Aldehyde dehydrogenase, mitochondrial
G: Aldehyde dehydrogenase, mitochondrial
H: Aldehyde dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)443,70069
Polymers435,7578
Non-polymers7,94361
Water48,2082676
1
A: Aldehyde dehydrogenase, mitochondrial
B: Aldehyde dehydrogenase, mitochondrial
C: Aldehyde dehydrogenase, mitochondrial
D: Aldehyde dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,75833
Polymers217,8784
Non-polymers3,88029
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30150 Å2
ΔGint-144 kcal/mol
Surface area56950 Å2
MethodPISA
2
E: Aldehyde dehydrogenase, mitochondrial
F: Aldehyde dehydrogenase, mitochondrial
G: Aldehyde dehydrogenase, mitochondrial
H: Aldehyde dehydrogenase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,94236
Polymers217,8784
Non-polymers4,06332
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30910 Å2
ΔGint-138 kcal/mol
Surface area56660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.216, 150.724, 177.299
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein
Aldehyde dehydrogenase, mitochondrial /


Mass: 54469.602 Da / Num. of mol.: 8 / Fragment: Mature sequence, residues 18-517 / Mutation: T244A
Source method: isolated from a genetically manipulated source
Details: lacks mitochondrial leader sequence / Source: (gene. exp.) Homo sapiens (human) / Gene: ALDH2, ALDM / Plasmid: pT-7-7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P05091, aldehyde dehydrogenase (NAD+)

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Non-polymers , 6 types, 2737 molecules

#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#3: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Na
#4: Chemical
ChemComp-GAI / GUANIDINE / Guanidine


Mass: 59.070 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: CH5N3
#5: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Nicotinamide adenine dinucleotide


Mass: 663.425 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Comment: NAD*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2676 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.18 Å3/Da / Density % sol: 43.59 %
Crystal growTemperature: 292 K / Method: vapor diffusion / pH: 6.4
Details: 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

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.54 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 7, 2007 / Details: Osmic Blue
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.25→50 Å / Num. obs: 179717 / % possible obs: 99.7 % / Redundancy: 4.4 % / Biso Wilson estimate: 35.5 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 16
Reflection shellResolution: 2.25→2.33 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.227 / Mean I/σ(I) obs: 4.8 / % possible all: 98.1

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMAC5.3.0037refinement
PDB_EXTRACT3.1data extraction
CrystalCleardata collection
REFMACphasing
RefinementMethod to determine structure: Direct Refinement
Starting model: PDB Entry 1o05
Resolution: 2.25→50 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.928 / Occupancy max: 1 / Occupancy min: 0.25 / SU B: 5.935 / SU ML: 0.15 / Cross valid method: THROUGHOUT / ESU R Free: 0.224 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.219 8995 5 %RANDOM
Rwork0.168 ---
obs0.17 179564 99.62 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso max: 58.12 Å2 / Biso mean: 25.611 Å2 / Biso min: 9.58 Å2
Baniso -1Baniso -2Baniso -3
1-3.36 Å20 Å20 Å2
2---2.02 Å20 Å2
3----1.34 Å2
Refinement stepCycle: LAST / Resolution: 2.25→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms30368 0 516 2676 33560
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02231813
X-RAY DIFFRACTIONr_angle_refined_deg1.0731.96643217
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.71354008
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.46224.6821414
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.893155096
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.72615160
X-RAY DIFFRACTIONr_chiral_restr0.070.24720
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0224420
X-RAY DIFFRACTIONr_nbd_refined0.1820.216358
X-RAY DIFFRACTIONr_nbtor_refined0.30.221980
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1210.23078
X-RAY DIFFRACTIONr_metal_ion_refined0.050.211
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1620.271
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1170.242
X-RAY DIFFRACTIONr_mcbond_it0.3131.519809
X-RAY DIFFRACTIONr_mcangle_it0.616231798
X-RAY DIFFRACTIONr_scbond_it1.139312510
X-RAY DIFFRACTIONr_scangle_it1.8964.511417
LS refinement shellResolution: 2.25→2.309 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.259 656 -
Rwork0.189 12119 -
all-12775 -
obs-12775 96.95 %

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