9h1m

Recombinant ferric horseradish peroxidase C1A

Method: X-RAY DIFFRACTION Dmax: 65.3 Å Quality: GOOD

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

Peroxidase C1A

Armoracia rusticana

UniProt P00433

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 31–338 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CA CALCIUM ION × 2 EDO 1,2-ETHANEDIOL × 5 2HP DIHYDROGENPHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277.15 K;25% (w/v) PEG 1500, 100 mM SPG (2:7:7, succinic acid:sodium hydrogen phosphate:glycine buffer pH 8.5 Resolution 1.63 Å R-free 0.189

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.

31 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PER1A_ARMRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–309; UniProt 31–338

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 9h1m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h1m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h1m
Deposition date deposition_date2024-10-09
Structure title titleRecombinant ferric horseradish peroxidase C1A
Keywords keywordsHorseradish Peroxidase, Ferric, oxidoreductases, Heme, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.09
Radius of gyration Rg (electron density) rg_electron19.03
Forward intensity I(0) i021762000.00
Molecular weight molecular_weight34803.0 kDa
Excluded volume excluded_volume43201 ų
Envelope volume envelope_volume47636 ų
Hydration-shell volume shell_volume20734 ų
Envelope diameter envelope_diameter66.6
Shell Rg shell_rg25.66
Envelope Rg envelope_rg19.39
Shape Rg shape_rg19.01
Total Rg total_rg19.94
Total atoms total_atoms2439
Residues n_residues306
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 dmax65.3
Rg (real space) rg_real20.02
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.1760e+07
I(0) uncertainty (real space) i0_real_error2.8190e+05
Rg (reciprocal space) rg_reciprocal20.03
I(0) (reciprocal space) i0_reciprocal21760000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.299
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5203000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)