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1cwn

CRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME

Method: X-RAY DIFFRACTION Dmax: 63.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALDEHYDE REDUCTASE

OrganismNot specified

UniProt P50578

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–324 Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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 1CWN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AE4 ALDEHYDE REDUCTASE COMPLEXED WITH COFACTOR AND INHIBITOR, ALPHA CARBON ATOMS ONLY Deposited 1997-03-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–324（324 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 TOL TOLRESTAT × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.9；BUFFERED AMMONIUM SULFATE SOLUTION, PH 8.9
Resolution 2.40 Å
1HQT THE CRYSTAL STRUCTURE OF AN ALDEHYDE REDUCTASE Y50F MUTANT-NADP COMPLEX AND ITS IMPLICATIONS FOR SUBSTRATE BINDING Deposited 2000-12-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–325（325 aa）
Mutation：Y50F NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；277 K；PEG 6000, NaCl, MES, EVAPORATION, temperature 277.0K
Resolution 2.20 Å R-free 0.296
3CV7 Crystal structure of porcine aldehyde reductase ternary complex Deposited 2008-04-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–325（325 aa）
Not recorded SO4 SULFATE ION × 4 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 C2U 3,5-dichloro-2-hydroxybenzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；2M ammonium sulphate, 0.1M tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 2.41 Å R-free 0.247
3FX4 Porcine aldehyde reductase in ternary complex with inhibitor Deposited 2009-01-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–325（325 aa）
Not recorded SO4 SULFATE ION × 3 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FX4 [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；2M ammonium sulphate, 0.1M tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
Resolution 1.99 Å R-free 0.246
3H4G Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor Fidarestat: Implications for inhibitor binding and selectivity Deposited 2009-04-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–325（325 aa）
Not recorded SO4 SULFATE ION × 1 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 FID (2S,4S)-2-AMINOFORMYL-6-FLUORO-SPIRO[CHROMAN-4,4'-IMIDAZOLIDINE]-2',5'-DIONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；295 K；2M ammonium sulphate, 0.1M tris, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.85 Å R-free 0.216

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AK1A1_PIG
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–324； UniProt 1–324

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 1cwn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cwn
Deposition date deposition_date1996-07-30
Structure title titleCRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME
Keywords keywordsTIM-BARREL, OXIDOREDUCTASE, NADP; 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_guinier19.63 Å
Radius of gyration Rg (electron density) rg_electron18.83 Å
Forward intensity I(0) i022664900.00
Molecular weight molecular_weight37152.0 kDa
Excluded volume excluded_volume45475 ų
Envelope volume envelope_volume32236 ų
Hydration-shell volume shell_volume15822 ų
Envelope diameter envelope_diameter58.6 Å
Shell Rg shell_rg22.85 Å
Envelope Rg envelope_rg17.52 Å
Shape Rg shape_rg18.20 Å
Total Rg total_rg19.29 Å
Total atoms total_atoms48
Residues n_residues—
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 dmax63.6 Å
Rg (real space) rg_real19.47 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real2.2660e+07
I(0) uncertainty (real space) i0_real_error2.5660e+05
Rg (reciprocal space) rg_reciprocal19.50 Å
I(0) (reciprocal space) i0_reciprocal22660000.0000
Solution quality estimate total_estimate0.7896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.0 Å
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.4050 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6502000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.760; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000
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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cwna_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
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8. Citations (2)

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9. Files and Curves (10)