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3h4g

Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor Fidarestat: Implications for inhibitor binding and selectivity

Method: X-RAY DIFFRACTION Dmax: 61.4 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Alcohol dehydrogenase [NADP+]

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 1–325 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

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 3H4G 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 construct 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
1CWN CRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME Deposited 1996-07-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–324（324 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1HQT THE CRYSTAL STRUCTURE OF AN ALDEHYDE REDUCTASE Y50F MUTANT-NADP COMPLEX AND ITS IMPLICATIONS FOR SUBSTRATE BINDING Deposited 2000-12-19 Different mutation/modification 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）
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 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 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

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 1–325； UniProt 1–325

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 3h4g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h4g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h4g
Deposition date deposition_date2009-04-20
Structure title titleStructure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor Fidarestat: Implications for inhibitor binding and selectivity
Keywords keywordsTIM BARREL, ALDO-KETO REDUCTASE, TERNARY COMPLEX, NADP, Oxidoreductase; 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_guinier20.00 Å
Radius of gyration Rg (electron density) rg_electron18.83 Å
Forward intensity I(0) i023499000.00
Molecular weight molecular_weight37058.0 kDa
Excluded volume excluded_volume46365 ų
Envelope volume envelope_volume51605 ų
Hydration-shell volume shell_volume22178 ų
Envelope diameter envelope_diameter61.7 Å
Shell Rg shell_rg25.91 Å
Envelope Rg envelope_rg19.13 Å
Shape Rg shape_rg18.83 Å
Total Rg total_rg19.76 Å
Total atoms total_atoms2610
Residues n_residues320
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 dmax61.4 Å
Rg (real space) rg_real19.88 Å
Rg uncertainty (real space) rg_real_error0.26 Å
I(0) (real space) i0_real2.3500e+07
I(0) uncertainty (real space) i0_real_error2.9940e+05
Rg (reciprocal space) rg_reciprocal19.90 Å
I(0) (reciprocal space) i0_reciprocal23500000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4 Å
Skewness Skewness skewness0.136
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.3950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7401000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.997
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3h4ga_
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)

CATH v4.4 (1 domains)

Domain ID domain_id3h4gA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
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8. Citations (1)

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9. Files and Curves (10)