1f25

CRYSTAL STRUCTURE OF NO COMPLEX OF THR243ASN MUTANTS OF CYTOCHROME P450NOR

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: GOOD

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

NITRIC OXIDE REDUCTASE

Fusarium oxysporum

UniProt P23295

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 1–402 Mutation:T243N HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NO NITRIC OXIDE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;PEG3350, MES, Glycerol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.40 Å R-free 0.204

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.

26 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NOR_FUSOX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–402; UniProt 1–402

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 1f25

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f25
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f25
Deposition date deposition_date2000-05-23
Structure title titleCRYSTAL STRUCTURE OF NO COMPLEX OF THR243ASN MUTANTS OF CYTOCHROME P450NOR
Keywords keywordsnitric oxide reductase, Cytochrome P450nor, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.14
Radius of gyration Rg (electron density) rg_electron21.07
Forward intensity I(0) i032757400.00
Molecular weight molecular_weight44771.0 kDa
Excluded volume excluded_volume56363 ų
Envelope volume envelope_volume65536 ų
Hydration-shell volume shell_volume25402 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg28.18
Envelope Rg envelope_rg21.17
Shape Rg shape_rg21.06
Total Rg total_rg22.00
Total atoms total_atoms3151
Residues n_residues399
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 dmax69.2
Rg (real space) rg_real21.98
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.2760e+07
I(0) uncertainty (real space) i0_real_error3.9580e+05
Rg (reciprocal space) rg_reciprocal22.01
I(0) (reciprocal space) i0_reciprocal32760000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.142
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6053000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1f25a_
Class classa — All alpha proteins
Fold Fold folda.104 — Cytochrome P450
Superfamily Superfamily superfamilya.104.1 — Cytochrome P450
Family Family familya.104.1.1 — Cytochrome P450

CATH v4.4 (1 domains)

Domain ID domain_id1f25A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology630 — Cytochrome p450
Homologous superfamily homologous superfamily10 — Cytochrome P450

8. Citations (3)

9. Files and Curves (10)