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1a4s

BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER

Method: X-RAY DIFFRACTION Dmax: 110.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BETAINE ALDEHYDE DEHYDROGENASE

OrganismNot specified

UniProt P56533

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 1–503 Chain B； UniProt 1–503 Chain C； UniProt 1–503 Chain D； UniProt 1–503 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；287 K；PROTEIN WAS CRYSTALLIZED AT 14 DEGREES FROM 20% PEG 4000, 9.5% ISOPROPANOL, 100 MM HEPES, PH 7.5, temperature 287K Resolution 2.10 Å R-free 0.253

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 1A4S Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BPW BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER Deposited 1998-08-12 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–503（503 aa）
Chain B 1–503（503 aa）
Chain C 1–503（503 aa）
Chain D 1–503（503 aa）
Not recorded NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；287 K；PROTEIN WAS CRYSTALLIZED AT 14 DEGREES FROM 20% PEG 4000, 9.5% ISOPROPANOL, 100 MM HEPES, PH 7.5, temperature 287K
Resolution 2.80 Å R-free 0.257

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

View Construct and Data Evidence
UniProt name BADH_GADCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–503； UniProt 1–503 Author chain B； PDBConstruct 1–503； UniProt 1–503 Author chain C； PDBConstruct 1–503； UniProt 1–503 Author chain D； PDBConstruct 1–503； UniProt 1–503

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 1a4s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a4s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a4s
Deposition date deposition_date1998-02-03
Structure title titleBETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER
Keywords keywordsOXIDOREDUCTASE, ALDEHYDE OXIDATION; 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_guinier37.46 Å
Radius of gyration Rg (electron density) rg_electron36.76 Å
Forward intensity I(0) i0703120000.00
Molecular weight molecular_weight217450.0 kDa
Excluded volume excluded_volume272500 ų
Envelope volume envelope_volume326840 ų
Hydration-shell volume shell_volume70280 ų
Envelope diameter envelope_diameter115.6 Å
Shell Rg shell_rg45.61 Å
Envelope Rg envelope_rg36.64 Å
Shape Rg shape_rg36.71 Å
Total Rg total_rg37.40 Å
Total atoms total_atoms15232
Residues n_residues2012
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 dmax110.4 Å
Rg (real space) rg_real37.17 Å
Rg uncertainty (real space) rg_real_error0.54 Å
I(0) (real space) i0_real7.0310e+08
I(0) uncertainty (real space) i0_real_error1.0910e+07
Rg (reciprocal space) rg_reciprocal37.36 Å
I(0) (reciprocal space) i0_reciprocal703200000.0000
Solution quality estimate total_estimate0.8913
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.3 Å
Skewness Skewness skewness0.056
Kurtosis Kurtosis kurtosis-0.584
Angular range angular_range— – 0.2100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118000000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.724
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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_idd1a4sa_
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_idd1a4sb_
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_idd1a4sc_
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_idd1a4sd_
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_id1a4sA01
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_id1a4sA02
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_id1a4sB01
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_id1a4sB02
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_id1a4sC01
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_id1a4sC02
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_id1a4sD01
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_id1a4sD02
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)