1cjc

STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS

Method: X-RAY DIFFRACTION Dmax: 78.4 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (ADRENODOXIN REDUCTASE)

Bos taurus

UniProt P08165

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 33–492 Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;DROPLET: 4 MG/ML PROTEIN, 8% PEG8000, 5% GLYCEROL, 100 MM CALCIUM ACETATE, 50 MM SODIUM-CACODYLATE PH 6.5. RESERVOIR: 12 % PEG8000, 100 MM CALCIUM ACETATE, 50 MM SODIUM CACODYLATE PH 6.5. Resolution 1.70 Å R-free 0.223

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADRO_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–460; UniProt 33–492

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 1cjc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cjc
Deposition date deposition_date1999-04-12
Structure title titleSTRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS
Keywords keywordsFLAVOENZYME, MAD ANALYSIS, ELECTRON TRANSFERASE, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.66
Radius of gyration Rg (electron density) rg_electron23.62
Forward intensity I(0) i043290500.00
Molecular weight molecular_weight50509.0 kDa
Excluded volume excluded_volume63149 ų
Envelope volume envelope_volume75466 ų
Hydration-shell volume shell_volume26642 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg30.83
Envelope Rg envelope_rg23.75
Shape Rg shape_rg23.61
Total Rg total_rg24.48
Total atoms total_atoms3558
Residues n_residues455
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax78.4
Rg (real space) rg_real24.59
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real4.3290e+07
I(0) uncertainty (real space) i0_real_error6.0960e+05
Rg (reciprocal space) rg_reciprocal24.61
I(0) (reciprocal space) i0_reciprocal43290000.0000
Solution quality estimate total_estimate0.9044
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.258
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10480000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cjca1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.1 — C-terminal domain of adrenodoxin reductase-like
Domain ID domain_idd1cjca2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.4 — Nucleotide-binding domain
Superfamily Superfamily superfamilyc.4.1 — Nucleotide-binding domain
Family Family familyc.4.1.1 — N-terminal domain of adrenodoxin reductase-like

CATH v4.4 (2 domains)

Domain ID domain_id1cjcA01
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_id1cjcA02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain

8. Citations (2)

9. Files and Curves (10)