1gx2

Recombinant horseradish peroxidase Phe209Ser complex with benzhydroxamic acid

Method: X-RAY DIFFRACTION Dmax: 83.9 Å Quality: EXCELLENT

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 Mutation:YES HEM PROTOPORPHYRIN IX CONTAINING FE × 1 BHO BENZHYDROXAMIC ACID × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.50 Resolution 2.20 Å R-free 0.197
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 31–338 Mutation:YES HEM PROTOPORPHYRIN IX CONTAINING FE × 1 BHO BENZHYDROXAMIC ACID × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.50 Resolution 2.20 Å R-free 0.197

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 33 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 2–309; UniProt 31–338 Author chain B; 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 1gx2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gx2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gx2
Deposition date deposition_date2002-03-26
Structure title titleRecombinant horseradish peroxidase Phe209Ser complex with benzhydroxamic acid
Keywords keywordsOXIDOREDUCTASE, PEROXIDASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.44
Radius of gyration Rg (electron density) rg_electron26.59
Forward intensity I(0) i082748100.00
Molecular weight molecular_weight69466.0 kDa
Excluded volume excluded_volume86182 ų
Envelope volume envelope_volume102490 ų
Hydration-shell volume shell_volume31921 ų
Envelope diameter envelope_diameter87.0
Shell Rg shell_rg34.13
Envelope Rg envelope_rg26.33
Shape Rg shape_rg26.60
Total Rg total_rg27.34
Total atoms total_atoms4872
Residues n_residues618
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 dmax83.9
Rg (real space) rg_real27.37
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real8.2750e+07
I(0) uncertainty (real space) i0_real_error1.2830e+06
Rg (reciprocal space) rg_reciprocal27.40
I(0) (reciprocal space) i0_reciprocal82750000.0000
Solution quality estimate total_estimate0.9103
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.573
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22320000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1gx2a_
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
Domain ID domain_idd1gx2b_
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 (4 domains)

Domain ID domain_id1gx2A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1gx2A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id1gx2B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1gx2B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2

8. Citations (4)

9. Files and Curves (10)