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1cwu

BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE

Method: X-RAY DIFFRACTION Dmax: 87.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ENOYL ACP REDUCTASE

Brassica napus

UniProt P80030

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 85–380 Chain B； UniProt 85–380 Mutation：A138G NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TDB 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.3；290 K；4.5 M NACL AND 50 MM NA ACETATE, pH 5.3, VAPOR DIFFUSION, HANGING DROP, temperature 17K Resolution 2.50 Å R-free 0.314

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 1CWU Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1D7O CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN Deposited 1999-10-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 84–380（297 aa）
Not recorded NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å R-free 0.225
1ENO BRASSICA NAPUS ENOYL ACP REDUCTASE/NAD BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE Deposited 1995-10-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 74–385（312 aa）
Mutation：S1A NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 1.90 Å
1ENP BRASSICA NAPUS ENOYL ACP REDUCTASE/NADH BINARY COMPLEX AT PH 8.0 AND ROOM TEMPERATURE Deposited 1995-10-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 74–385（312 aa）
Mutation：S1A NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FABI_BRANA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–296； UniProt 85–380 Author chain B； PDBConstruct 1–296； UniProt 85–380

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 1cwu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cwu
Deposition date deposition_date1999-08-26
Structure title titleBRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE
Keywords keywordsOXIDOREDUCTASE, PLANT LIPID BIOSYNTHESIS, DIAZABORINE; 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_guinier25.87 Å
Radius of gyration Rg (electron density) rg_electron24.92 Å
Forward intensity I(0) i065478000.00
Molecular weight molecular_weight63090.0 kDa
Excluded volume excluded_volume78899 ų
Envelope volume envelope_volume90231 ų
Hydration-shell volume shell_volume30065 ų
Envelope diameter envelope_diameter91.8 Å
Shell Rg shell_rg32.40 Å
Envelope Rg envelope_rg25.18 Å
Shape Rg shape_rg24.96 Å
Total Rg total_rg25.60 Å
Total atoms total_atoms4441
Residues n_residues592
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 dmax87.7 Å
Rg (real space) rg_real25.86 Å
Rg uncertainty (real space) rg_real_error0.73 Å
I(0) (real space) i0_real6.5480e+07
I(0) uncertainty (real space) i0_real_error1.1200e+06
Rg (reciprocal space) rg_reciprocal25.87 Å
I(0) (reciprocal space) i0_reciprocal65480000.0000
Solution quality estimate total_estimate0.8730
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.2 Å
Skewness Skewness skewness0.383
Kurtosis Kurtosis kurtosis-0.218
Angular range angular_range— – 0.3050 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9498000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.950
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cwua_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.2 — Tyrosine-dependent oxidoreductases
Domain ID domain_idd1cwub_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.2 — Tyrosine-dependent oxidoreductases

CATH v4.4 (2 domains)

Domain ID domain_id1cwuA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1cwuB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
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8. Citations (1)

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9. Files and Curves (10)