1a8s

CHLOROPEROXIDASE F/PROPIONATE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 56.0 Å Quality: GOOD

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

CHLOROPEROXIDASE F

Pseudomonas fluorescens

UniProt O31158

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 1–273 Not recorded SO4 SULFATE ION × 4 PPI PROPANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.6;1.0 M AMMONIUM SULFATE 50MM CITRATE/PHOSPHATE BUFFER PH 6.6 Resolution 1.80 Å R-free 0.205
2 Protein homooligomer Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–273 Not recorded SO4 SULFATE ION × 48 PPI PROPANOIC ACID × 12 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.6;1.0 M AMMONIUM SULFATE 50MM CITRATE/PHOSPHATE BUFFER PH 6.6 Resolution 1.80 Å R-free 0.205
3 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–273 Not recorded SO4 SULFATE ION × 12 PPI PROPANOIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.6;1.0 M AMMONIUM SULFATE 50MM CITRATE/PHOSPHATE BUFFER PH 6.6 Resolution 1.80 Å R-free 0.205

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PRXC_PSEFL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–273; UniProt 1–273

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 1a8s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a8s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a8s
Deposition date deposition_date1998-03-27
Structure title titleCHLOROPEROXIDASE F/PROPIONATE COMPLEX
Keywords keywordsHALOPEROXIDASE, OXIDOREDUCTASE, PROPIONATE COMPLEX; HALOPEROXIDASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.33
Radius of gyration Rg (electron density) rg_electron17.10
Forward intensity I(0) i016517300.00
Molecular weight molecular_weight29971.0 kDa
Excluded volume excluded_volume37101 ų
Envelope volume envelope_volume40625 ų
Hydration-shell volume shell_volume19258 ų
Envelope diameter envelope_diameter57.0
Shell Rg shell_rg23.99
Envelope Rg envelope_rg17.39
Shape Rg shape_rg17.06
Total Rg total_rg18.15
Total atoms total_atoms2110
Residues n_residues273
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 dmax56.0
Rg (real space) rg_real18.18
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.6520e+07
I(0) uncertainty (real space) i0_real_error1.9790e+05
Rg (reciprocal space) rg_reciprocal18.20
I(0) (reciprocal space) i0_reciprocal16520000.0000
Solution quality estimate total_estimate0.8965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.066
Kurtosis Kurtosis kurtosis-0.445
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3691000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a8sa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.12 — Haloperoxidase

CATH v4.4 (1 domains)

Domain ID domain_id1a8sA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain

8. Citations (1)

9. Files and Curves (10)