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1a8u

CHLOROPEROXIDASE T/BENZOATE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 93.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CHLOROPEROXIDASE T

Streptomyces aureofaciens

UniProt O31168

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 2–278 Chain B； UniProt 2–278 Not recorded SO4 SULFATE ION × 5 BEZ BENZOIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.8；1.8 M AMMONIUM SULFATE PH 7.8., SMALL AMOUNTS OF SOLID SODIUM BENZOATE Resolution 1.60 Å R-free 0.171

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.

Other PDB Difference from Current Entry 1A8U Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A7U CHLOROPEROXIDASE T Deposited 1998-03-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–278（277 aa）
Chain B 2–278（277 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.8；1.8 M AMMONIUM SULFATE PH 7.8.
Resolution 1.75 Å R-free 0.176

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRXC_STRAU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–277； UniProt 2–278 Author chain B； PDBConstruct 1–277； UniProt 2–278

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 1a8u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a8u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a8u
Deposition date deposition_date1998-03-26
Structure title titleCHLOROPEROXIDASE T/BENZOATE COMPLEX
Keywords keywordsHALOPEROXIDASE, OXIDOREDUCTASE, BENZOATE COMPLEX; HALOPEROXIDASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.99 Å
Radius of gyration Rg (electron density) rg_electron28.29 Å
Forward intensity I(0) i060921200.00
Molecular weight molecular_weight61138.0 kDa
Excluded volume excluded_volume76212 ų
Envelope volume envelope_volume90402 ų
Hydration-shell volume shell_volume27377 ų
Envelope diameter envelope_diameter95.2 Å
Shell Rg shell_rg34.57 Å
Envelope Rg envelope_rg28.06 Å
Shape Rg shape_rg28.29 Å
Total Rg total_rg28.92 Å
Total atoms total_atoms4333
Residues n_residues554
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax93.5 Å
Rg (real space) rg_real29.08 Å
Rg uncertainty (real space) rg_real_error0.68 Å
I(0) (real space) i0_real6.0920e+07
I(0) uncertainty (real space) i0_real_error8.4650e+05
Rg (reciprocal space) rg_reciprocal29.05 Å
I(0) (reciprocal space) i0_reciprocal60920000.0000
Solution quality estimate total_estimate0.8578
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.2 Å
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.669
Angular range angular_range— – 0.2750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27940000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.860; Smooth: 0.899
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a8ua_
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
Domain ID domain_idd1a8ub_
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 (2 domains)

Domain ID domain_id1a8uA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id1a8uB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
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8. Citations (1)

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9. Files and Curves (10)