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1ag8

ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA

Method: X-RAY DIFFRACTION Dmax: 110.5 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALDEHYDE DEHYDROGENASE

OrganismNot specified

UniProt P20000

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 22–520 Chain B； UniProt 22–520 Chain C； UniProt 22–520 Chain D； UniProt 22–520 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；14% PEG 8000, 100 MM MES, PH 6.5, 0.2 MM MGCL2, 1MM NAD; THEN SOAKED IN SAME SOLUTION WITHOUT NAD OR MGCL2 FOR 1 WEEK. Resolution 2.65 Å R-free 0.282

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 1AG8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A4Z ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III) Deposited 1998-02-10 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 22–520（499 aa） Fragment：NAD BINDING DOMAIN
Chain B 22–520（499 aa） Fragment：NAD BINDING DOMAIN
Chain C 22–520（499 aa） Fragment：NAD BINDING DOMAIN
Chain D 22–520（499 aa） Fragment：NAD BINDING DOMAIN
Not recorded SM SAMARIUM (III) ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；14% PEG 8000, 100 MM MES, PH 6.5, 0.2 MM MGCL2, 1MM NAD; THEN SOAKED IN 1 MM SMCL3 OVERNIGHT.
Resolution 2.75 Å R-free 0.302

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ALDH2_BOVIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–499； UniProt 22–520 Author chain B； PDBConstruct 1–499； UniProt 22–520 Author chain C； PDBConstruct 1–499； UniProt 22–520 Author chain D； PDBConstruct 1–499； UniProt 22–520

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 1ag8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ag8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ag8
Deposition date deposition_date1997-04-03
Structure title titleALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
Keywords keywordsOXIDOREDUCTASE, ALCOHOL METABOLISM, ALDEHYDE OXIDATION, ALPHA/BETA DOMAIN, DEHYDROGENASE; 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_guinier36.55 Å
Radius of gyration Rg (electron density) rg_electron35.85 Å
Forward intensity I(0) i0681596000.00
Molecular weight molecular_weight215610.0 kDa
Excluded volume excluded_volume270550 ų
Envelope volume envelope_volume314250 ų
Hydration-shell volume shell_volume68922 ų
Envelope diameter envelope_diameter112.0 Å
Shell Rg shell_rg45.17 Å
Envelope Rg envelope_rg35.80 Å
Shape Rg shape_rg35.83 Å
Total Rg total_rg36.43 Å
Total atoms total_atoms15196
Residues n_residues1972
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 dmax110.5 Å
Rg (real space) rg_real36.28 Å
Rg uncertainty (real space) rg_real_error0.77 Å
I(0) (real space) i0_real6.8160e+08
I(0) uncertainty (real space) i0_real_error1.0700e+07
Rg (reciprocal space) rg_reciprocal36.45 Å
I(0) (reciprocal space) i0_reciprocal681700000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.3 Å
Skewness Skewness skewness0.064
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_alpha128700000.0000
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: 0.975; Smooth: 0.936
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1ag8a_
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_idd1ag8b_
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_idd1ag8c_
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_idd1ag8d_
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_id1ag8A01
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_id1ag8A02
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_id1ag8B01
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_id1ag8B02
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_id1ag8C01
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_id1ag8C02
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_id1ag8D01
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_id1ag8D02
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)