SAXSdb — 1bro

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

BROMOPEROXIDASE A2

Streptomyces aureofaciens

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 1–277	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；1.8 M AMMONIUM SULFATE PH 8.0.	Resolution 2.05 Å
2	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 1–277	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；1.8 M AMMONIUM SULFATE PH 8.0.	Resolution 2.05 Å

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 1BRO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BRT BROMOPEROXIDASE A2 MUTANT M99T Deposited 1998-03-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–277（277 aa）	Mutation：M99T	CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；1.8 M AMMONIUM SULFATE 0.1 M TRIS/HCL, PH 8.5.	Resolution 1.50 Å R-free 0.164
3VDX Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains Deposited 2012-01-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Chain B 1–278（278 aa） Chain C 1–278（278 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.3；298 K；1.2M NaH2PO4, 0.8M K2HPO4, 0.1M CAPS, pH 10.3, vapor diffusion, hanging drop, temperature 298K	Resolution 3.00 Å R-free 0.281
4D9J Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains Deposited 2012-01-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Chain B 1–278（278 aa） Chain C 1–278（278 aa） Chain D 1–278（278 aa） Chain E 1–278（278 aa） Chain F 1–278（278 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.3；298 K；1.2M NaH2PO4, 0.8M K2HPO4, 0.1M CAPS, pH 10.3, vapor diffusion, hanging drop, temperature 298K	Resolution 3.92 Å R-free 0.294
4D9J Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains Deposited 2012-01-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain G 1–278（278 aa） Chain H 1–278（278 aa） Chain I 1–278（278 aa） Chain J 1–278（278 aa） Chain K 1–278（278 aa） Chain L 1–278（278 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.3；298 K；1.2M NaH2PO4, 0.8M K2HPO4, 0.1M CAPS, pH 10.3, vapor diffusion, hanging drop, temperature 298K	Resolution 3.92 Å R-free 0.294
4IQ4 Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P21212 form Deposited 2013-01-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Chain B 1–278（278 aa） Chain C 1–278（278 aa） Chain D 1–278（278 aa） Chain E 1–278（278 aa） Chain F 1–278（278 aa）	Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；298 K；0.1M Na Citrate pH 4.4, 10% PEG 3,000, vapor diffusion, hanging drop, temperature 298K	Resolution 3.50 Å R-free 0.231
4ITV Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P212121 form Deposited 2013-01-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Chain B 1–278（278 aa） Chain C 1–278（278 aa） Chain D 1–278（278 aa） Chain E 1–278（278 aa） Chain F 1–278（278 aa） Chain G 1–278（278 aa） Chain H 1–278（278 aa） Chain I 1–278（278 aa） Chain J 1–278（278 aa） Chain K 1–278（278 aa） Chain L 1–278（278 aa）	Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；298 K；0.1M Na Citrate pH 4.4, 10% PEG 3000, vapor diffusion, hanging drop, temperature 298K	Resolution 3.60 Å R-free 0.240
4IVJ Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, I222 form Deposited 2013-01-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Chain B 1–278（278 aa） Chain C 1–278（278 aa）	Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T Mutation：K118A, L279Q, Q24T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；298 K；0.1M Na Citrate pH 4.4, 10% PEG 3000, vapor diffusion, hanging drop, temperature 298K	Resolution 7.35 Å R-free 0.288
4QES Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, I222 form Deposited 2014-05-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Fragment：SEE REMARK 999 Chain B 1–278（278 aa） Fragment：SEE REMARK 999 Chain C 1–278（278 aa） Fragment：SEE REMARK 999	Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；298 K；0.1 M sodium citrate, pH 4.4, 11% PEG3000, 200 mM sodium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 4.19 Å R-free 0.295
4QF0 Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, P21212 form Deposited 2014-05-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Fragment：SEE REMARK 999 Chain B 1–278（278 aa） Fragment：SEE REMARK 999 Chain C 1–278（278 aa） Fragment：SEE REMARK 999 Chain D 1–278（278 aa） Fragment：SEE REMARK 999 Chain E 1–278（278 aa） Fragment：SEE REMARK 999 Chain F 1–278（278 aa） Fragment：SEE REMARK 999	Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；0.1 M Tris, pH 7.0, 10% PEG8000, 0.2 M magnesium chloride, 3% trehalose, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 6.49 Å R-free 0.324
4QFF Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, P212121 form Deposited 2014-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–278（278 aa） Fragment：SEE REMARK 999 Chain B 1–278（278 aa） Fragment：SEE REMARK 999 Chain C 1–278（278 aa） Fragment：SEE REMARK 999 Chain D 1–278（278 aa） Fragment：SEE REMARK 999 Chain E 1–278（278 aa） Fragment：SEE REMARK 999 Chain F 1–278（278 aa） Fragment：SEE REMARK 999 Chain G 1–278（278 aa） Fragment：SEE REMARK 999 Chain H 1–278（278 aa） Fragment：SEE REMARK 999 Chain I 1–278（278 aa） Fragment：SEE REMARK 999 Chain J 1–278（278 aa） Fragment：SEE REMARK 999 Chain K 1–278（278 aa） Fragment：SEE REMARK 999 Chain L 1–278（278 aa） Fragment：SEE REMARK 999	Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A Mutation：K118A, L279Q, Q24T, Y51A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；298 K；0.1 M sodium/potassium phosphate, pH 5.8, 10% PEG8000, 0.2 M sodium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 7.81 Å R-free 0.339

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BPOA2_STRAU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–277； UniProt 1–277 Author chain B； PDBConstruct 1–277； UniProt 1–277

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	1bro
Deposition date deposition_date	1996-06-01
Structure title title	BROMOPEROXIDASE A2
Keywords keywords	ANTIBIOTIC BIOSYNTHESIS, OXIDOREDUCTASE, PEROXIDASE, ALPHA/BETA HYDROLASE FOLD, HALOPEROXIDASE; 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	29.12 Å
Radius of gyration Rg (electron density) rg_electron	28.42 Å
Forward intensity I(0) i0	58621800.00
Molecular weight molecular_weight	60471.0 kDa
Excluded volume excluded_volume	75606 Å³
Envelope volume envelope_volume	90632 Å³
Hydration-shell volume shell_volume	27392 Å³
Envelope diameter envelope_diameter	94.8 Å
Shell Rg shell_rg	34.71 Å
Envelope Rg envelope_rg	28.09 Å
Shape Rg shape_rg	28.41 Å
Total Rg total_rg	29.05 Å
Total atoms total_atoms	4294
Residues n_residues	554
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	91.7 Å
Rg (real space) rg_real	29.22 Å
Rg uncertainty (real space) rg_real_error	0.72 Å
I(0) (real space) i0_real	5.8620e+07
I(0) uncertainty (real space) i0_real_error	8.7930e+05
Rg (reciprocal space) rg_reciprocal	29.18 Å
I(0) (reciprocal space) i0_reciprocal	58620000.0000
Solution quality estimate total_estimate	0.8642
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.2 Å
Skewness Skewness skewness	0.367
Kurtosis Kurtosis kurtosis	-0.660
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	22950000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.767

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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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1broa_
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	d1brob_
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 (2 domains)

Domain ID domain_id	1broA00
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	1broB00
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 (3)

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Unit-cell length a length_a	126.500 Å
Unit-cell length b length_b	126.500 Å
Unit-cell length c length_c	126.500 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	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Description description	BROMOPEROXIDASE A2
Molecular weight formula_weight	30278.4 kDa
EC 编号 ec_number	1.11.1.-
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4529

BROMOPEROXIDASE A2

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

BROMOPEROXIDASE A2

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (3)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Streptomyces aureofaciens
NCBI Class编号 ncbi_taxonomy_id	1894
宿主生物 host_organism	Streptomyces lividans

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	235

fit	/app/data/saxs_computation/br/1bro/1bro.fit
pddf	/app/data/pr_computation/br/1bro/1bro.pr.out
profile	/app/data/saxs_computation/br/1bro/1bro.dat