1w4w

Ferric horseradish peroxidase C1A in complex with formate

Method: X-RAY DIFFRACTION Dmax: 65.7 Å Quality: GOOD

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

HORSERADISH 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 31–353 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CA CALCIUM ION × 2 FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;20% PEG8000, 0.2M CA-ACETATE, 0.1 M NA-CACODYLATE PH 6.5, FERULIC ACID AS ADDITIVE STREAK SEEDING, HANGING DROP, 4DEGC Resolution 1.55 Å R-free 0.215

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 PERA_ARMRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–323; UniProt 31–353

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 1w4w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w4w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1w4w
Deposition date deposition_date2004-08-03
Structure title titleFerric horseradish peroxidase C1A in complex with formate
Keywords keywords;OXIDOREDUCTASE, FORMATE ION, CALCIUM, FERRIC STATE, GLYCOPROTEIN, HEME, HORSERADISH, IRON, MULTIGENE FAMILY, PEROXIDASE, PYRROLIDONE CARBOXYLIC ACID ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.06
Radius of gyration Rg (electron density) rg_electron19.01
Forward intensity I(0) i021267800.00
Molecular weight molecular_weight34442.0 kDa
Excluded volume excluded_volume42787 ų
Envelope volume envelope_volume46797 ų
Hydration-shell volume shell_volume20491 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg25.58
Envelope Rg envelope_rg19.30
Shape Rg shape_rg18.98
Total Rg total_rg19.93
Total atoms total_atoms2417
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 dmax65.7
Rg (real space) rg_real20.00
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.1270e+07
I(0) uncertainty (real space) i0_real_error2.4640e+05
Rg (reciprocal space) rg_reciprocal20.01
I(0) (reciprocal space) i0_reciprocal21270000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5211000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1w4wa_
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.1 — CCP-like

CATH v4.4 (2 domains)

Domain ID domain_id1w4wA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1w4wA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2

8. Citations (3)

9. Files and Curves (10)