SAXSdb — 7okw

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

Serine/threonine-protein kinase OSR1

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 423–527 Chain B； UniProt 423–527	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 CA CALCIUM ION × 1 MG MAGNESIUM ION × 2 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；278 K；Morpheus A8: 0.06 M Divalents 0.1 M Buffer System 2 7.5 37.5 % v/v Precipitant Mix 4. Divalents:Mg chloride; Ca chloride. Buffer: pH 7.5 Sodium HEPES; MOPS (acid). Precipitants: 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350.	Resolution 1.62 Å R-free 0.216

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 7OKW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2V3S Structural insights into the recognition of substrates and activators by the OSR1 kinase Deposited 2007-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 433–527（95 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.70 Å R-free 0.239
2V3S Structural insights into the recognition of substrates and activators by the OSR1 kinase Deposited 2007-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 433–527（95 aa）	Not recorded	ACT ACETATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.70 Å R-free 0.239
2VWI Structure of the OSR1 kinase, a hypertension drug target Deposited 2008-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303 Chain B 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303 Chain C 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303 Chain D 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303	Not recorded	AU GOLD ION × 11 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.287
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295 Chain B 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295 Chain C 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295 Chain D 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.25 Å R-free 0.267
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295 Chain D 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.25 Å R-free 0.267
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295 Chain C 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.25 Å R-free 0.267

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	OXSR1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–106； UniProt 423–527 Author chain B； PDBConstruct 2–106； UniProt 423–527

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	7okw
Deposition date deposition_date	2021-05-18
Structure title title	1.62A X-ray crystal structure of the conserved C-terminal (CCT) of human OSR1
Keywords keywords	KINASE, TRANSFERASE, CCT, SIGNALING PROTEIN; SIGNALING PROTEIN
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	18.49 Å
Radius of gyration Rg (electron density) rg_electron	17.33 Å
Forward intensity I(0) i0	7828910.00
Molecular weight molecular_weight	20907.0 kDa
Excluded volume excluded_volume	26419 Å³
Envelope volume envelope_volume	31510 Å³
Hydration-shell volume shell_volume	15528 Å³
Envelope diameter envelope_diameter	55.9 Å
Shell Rg shell_rg	23.00 Å
Envelope Rg envelope_rg	17.56 Å
Shape Rg shape_rg	17.30 Å
Total Rg total_rg	18.40 Å
Total atoms total_atoms	1469
Residues n_residues	194
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	57.3 Å
Rg (real space) rg_real	18.43 Å
Rg uncertainty (real space) rg_real_error	0.28 Å
I(0) (real space) i0_real	7.8290e+06
I(0) uncertainty (real space) i0_real_error	8.3090e+04
Rg (reciprocal space) rg_reciprocal	18.44 Å
I(0) (reciprocal space) i0_reciprocal	7829000.0000
Solution quality estimate total_estimate	0.8997
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.4 Å
Skewness Skewness skewness	0.208
Kurtosis Kurtosis kurtosis	-0.513
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2171000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.948

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Serine/threonine-protein kinase OSR1
Molecular weight formula_weight	11295.7 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1733

GSGSGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS

来源 Source

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

Entity 2 Entity 2 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	179

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8. Citations (1)

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Unit-cell length a length_a	70.168 Å
Unit-cell length b length_b	49.424 Å
Unit-cell length c length_c	56.439 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	99.44 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	monoclinic

Resolution resolution	1.620 Å
Low-resolution limit resolution_low	34.610 Å
R factor r_factor	0.1856
R_work r_work	0.1840
R_free r_free	0.2165

fit	/app/data/saxs_computation/ok/7okw/7okw.fit
pddf	/app/data/pr_computation/ok/7okw/7okw.pr.out
profile	/app/data/saxs_computation/ok/7okw/7okw.dat

1.62A X-ray crystal structure of the conserved C-terminal (CCT) of human OSR1

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

Serine/threonine-protein kinase OSR1

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