SAXSdb — 1a88

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

CHLOROPEROXIDASE L

Streptomyces lividans

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–275 Chain B； UniProt 1–275 Chain C； UniProt 1–275	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.2；2.0 M AMMONIUM SULFATE 100MM TRIS/HCL PH 8.2	Resolution 1.90 Å R-free 0.193

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_STRLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–275； UniProt 1–275 Author chain B； PDBConstruct 1–275； UniProt 1–275 Author chain C； PDBConstruct 1–275； UniProt 1–275

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1a88
Deposition date deposition_date	1998-04-03
Structure title title	CHLOROPEROXIDASE L
Keywords keywords	HALOPEROXIDASE, OXIDOREDUCTASE; HALOPEROXIDASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	28.02 Å
Radius of gyration Rg (electron density) rg_electron	27.22 Å
Forward intensity I(0) i0	132541000.00
Molecular weight molecular_weight	89302.0 kDa
Excluded volume excluded_volume	110770 Å³
Envelope volume envelope_volume	128920 Å³
Hydration-shell volume shell_volume	38202 Å³
Envelope diameter envelope_diameter	87.5 Å
Shell Rg shell_rg	35.73 Å
Envelope Rg envelope_rg	27.40 Å
Shape Rg shape_rg	27.18 Å
Total Rg total_rg	28.10 Å
Total atoms total_atoms	6315
Residues n_residues	825
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	86.1 Å
Rg (real space) rg_real	27.87 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	1.3250e+08
I(0) uncertainty (real space) i0_real_error	1.6760e+06
Rg (reciprocal space) rg_reciprocal	27.92 Å
I(0) (reciprocal space) i0_reciprocal	132500000.0000
Solution quality estimate total_estimate	0.9071
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	33.2 Å
Skewness Skewness skewness	0.181
Kurtosis Kurtosis kurtosis	-0.565
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	82130000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.964

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1a88a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.12 — Haloperoxidase

Domain ID domain_id	d1a88b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.12 — Haloperoxidase

Domain ID domain_id	d1a88c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.12 — Haloperoxidase

CATH v4.4 (3 domains)

Domain ID domain_id	1a88A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

Domain ID domain_id	1a88B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

Domain ID domain_id	1a88C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

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8. Citations (1)

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Unit-cell length a length_a	176.500 Å
Unit-cell length b length_b	176.500 Å
Unit-cell length c length_c	64.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	I 4
Space-group number int_tables_number	79
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	130.000 Å
R factor r_factor	0.1600
R_work r_work	0.1600
R_free r_free	0.1930

Description description	CHLOROPEROXIDASE L
Molecular weight formula_weight	29816.2 kDa
EC 编号 ec_number	1.11.1.10
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	6822

CHLOROPEROXIDASE L

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

CHLOROPEROXIDASE L

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Streptomyces lividans
NCBI Class编号 ncbi_taxonomy_id	1916
宿主生物 host_organism	Streptomyces aureofaciens

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	507

fit	/app/data/saxs_computation/a8/1a88/1a88.fit
pddf	/app/data/pr_computation/a8/1a88/1a88.pr.out
profile	/app/data/saxs_computation/a8/1a88/1a88.dat