SAXSdb — 1buo

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

PROTEIN (PROMYELOCYTIC LEUKEMIA ZINC FINGER PROTEIN PLZF)

Homo sapiens

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 6–126	Fragment：BTB DOMAIN	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；0.15 M CACL2, 0.1 M HEPES (PH 7.5), 4% ISOPROPANOL,	Resolution 1.90 Å R-free 0.252

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 1BUO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CS3 STRUCTURE OF BTB/POZ TRANSCRIPTION REPRESSION DOMAIN FROM PROMELOCYTIC LEUKEMIA ZINC FINGER ONCOPROTEIN Deposited 1999-08-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 7–122（116 aa） Fragment：BTB/POZ	Not recorded	MG MAGNESIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；VAPOR DIFFUSION BY 8% ISOPROPANOL, 600mM MAGNESIUM CHLORIDE, 50mM HEPES 7.5 and 50mM TRIS 8.5, pH 8.00	Resolution 2.00 Å R-free 0.272
1CS3 STRUCTURE OF BTB/POZ TRANSCRIPTION REPRESSION DOMAIN FROM PROMELOCYTIC LEUKEMIA ZINC FINGER ONCOPROTEIN Deposited 1999-08-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 7–122（116 aa） Fragment：BTB/POZ	Not recorded	MG MAGNESIUM ION × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；VAPOR DIFFUSION BY 8% ISOPROPANOL, 600mM MAGNESIUM CHLORIDE, 50mM HEPES 7.5 and 50mM TRIS 8.5, pH 8.00	Resolution 2.00 Å R-free 0.272
8YTH Crystal structures of human IRF2BP2 RING domain in complex with ZBTB16 peptide Deposited 2024-03-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 285–292（8 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M potassium thiocyanate and 30% (w/v) PEG MME 2000	Resolution 2.40 Å R-free 0.281

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ZBT16_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–121； UniProt 6–126

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	1buo
Deposition date deposition_date	1998-09-04
Structure title title	BTB DOMAIN FROM PLZF
Keywords keywords	;PROTEIN-PROTEIN INTERACTION DOMAIN, TRANSCRIPTIONAL REPRESSOR, ZINC-FINGER PROTEIN, PROTEIN STRUCTURE, PROMYELOCYTIC LEUKEMIA, GENE REGULATION ;; GENE REGULATION
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	17.46 Å
Radius of gyration Rg (electron density) rg_electron	16.46 Å
Forward intensity I(0) i0	3870240.00
Molecular weight molecular_weight	13906.0 kDa
Excluded volume excluded_volume	17441 Å³
Envelope volume envelope_volume	22241 Å³
Hydration-shell volume shell_volume	12236 Å³
Envelope diameter envelope_diameter	65.6 Å
Shell Rg shell_rg	21.43 Å
Envelope Rg envelope_rg	18.10 Å
Shape Rg shape_rg	16.33 Å
Total Rg total_rg	17.84 Å
Total atoms total_atoms	972
Residues n_residues	121
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	65.9 Å
Rg (real space) rg_real	17.61 Å
Rg uncertainty (real space) rg_real_error	0.58 Å
I(0) (real space) i0_real	3.8700e+06
I(0) uncertainty (real space) i0_real_error	5.0630e+04
Rg (reciprocal space) rg_reciprocal	17.59 Å
I(0) (reciprocal space) i0_reciprocal	3870000.0000
Solution quality estimate total_estimate	0.7894
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.3 Å
Skewness Skewness skewness	0.644
Kurtosis Kurtosis kurtosis	0.478
Angular range angular_range	— – 0.4550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	449400.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.528; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.738; Smooth: 0.937

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1buoa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.42 — POZ domain
Superfamily Superfamily superfamily	d.42.1 — POZ domain
Family Family family	d.42.1.1 — BTB/POZ domain

CATH v4.4 (1 domains)

Domain ID domain_id	1buoA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily	10 — Potassium Channel Kv1.1; Chain A

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8. Citations (1)

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Unit-cell length a length_a	72.630 Å
Unit-cell length b length_b	72.630 Å
Unit-cell length c length_c	168.980 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	16

Space group space_group	I 41 2 2
Space-group number int_tables_number	98
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2120
R_free r_free	0.2520

Description description	PROTEIN (PROMYELOCYTIC LEUKEMIA ZINC FINGER PROTEIN PLZF)
Molecular weight formula_weight	13927.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1101

BTB DOMAIN FROM PLZF

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

PROTEIN (PROMYELOCYTIC LEUKEMIA ZINC FINGER PROTEIN PLZF)

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	129

fit	/app/data/saxs_computation/bu/1buo/1buo.fit
pddf	/app/data/pr_computation/bu/1buo/1buo.pr.out
profile	/app/data/saxs_computation/bu/1buo/1buo.dat