SAXSdb — 8a5j

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

Serine/threonine-protein kinase 4 37kDa subunit

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 28–309 Chain B； UniProt 28–309	Non-standard monomer：Yes (specific site not provided by mmCIF)	5BS 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2M Ammonium citrate pH 7.0, 18% PEG3350	Resolution 2.12 Å R-free 0.248

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 8A5J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2JO8 Solution structure of C-terminal domain of human mammalian sterile 20-like kinase 1 (MST1) Deposited 2007-02-26	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 432–480（49 aa） Fragment：C-terminal SARAH domain, database residues 432-480 Chain B 432–480（49 aa） Fragment：C-terminal SARAH domain, database residues 432-480	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 125；Pressure AMBIENT NMR sample composition 1 mM [U-13C; U-15N] c-terminal domain of Mammalian sterile 20-like kinase 1, 100 mM sodium chloride, 2 mM DTT, 25 mM HEPES, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3COM Crystal structure of Mst1 kinase Deposited 2008-03-28	Different construct Different mutation/modification 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 2–311（310 aa） Fragment：Protein kinase domain: Residues 2-311	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.5；294 K；1700mM Ammonium sulfate, 300mM Lithium sulfate, 100mM CAPS pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 2.20 Å R-free 0.244
3COM Crystal structure of Mst1 kinase Deposited 2008-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–311（310 aa） Fragment：Protein kinase domain: Residues 2-311	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.5；294 K；1700mM Ammonium sulfate, 300mM Lithium sulfate, 100mM CAPS pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 2.20 Å R-free 0.244
4NR2 Crystal structure of STK4 (MST1) SARAH domain Deposited 2013-11-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480 Chain B 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480	Not recorded	EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；277.15 K；2.3M sodium formate, 0.1M acetate pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.240
4NR2 Crystal structure of STK4 (MST1) SARAH domain Deposited 2013-11-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480 Chain D 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；277.15 K；2.3M sodium formate, 0.1M acetate pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.240
4NR2 Crystal structure of STK4 (MST1) SARAH domain Deposited 2013-11-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480 Chain F 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；277.15 K；2.3M sodium formate, 0.1M acetate pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.240
4NR2 Crystal structure of STK4 (MST1) SARAH domain Deposited 2013-11-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480 Chain H 432–480（49 aa） Fragment：SARAH domain, UNP residues 432-480	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；277.15 K；2.3M sodium formate, 0.1M acetate pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.00 Å R-free 0.240
4OH8 Crystal Structure of the human MST1-RASSF5 SARAH heterodimer Deposited 2014-01-17	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 432–480（49 aa） Fragment：MST1 SARAH domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；35% (v/v) 2-methyl-2,4-pentanediol (MPD) acetate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.28 Å R-free 0.278
6YAT Crystal structure of STK4 (MST1) in complex with compound 6 Deposited 2020-03-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–311（311 aa） Chain B 1–311（311 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	3FX (2R)-3-(cyclohexylamino)-2-hydroxypropane-1-sulfonic acid × 1 GOL GLYCEROL × 7 OJ5 4-[5-(3-chlorophenyl)-7~{H}-pyrrolo[2,3-d]pyrimidin-4-yl]morpholine × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 11；293.15 K；0.6 M ammonium sulfate, 0.1 M lithium sulfate and 0.1 M CAPS, pH 11.0	Resolution 2.58 Å R-free 0.259
8PAV Crystal structure of MST1 with a MAP4K1 SMOL inhibitor Deposited 2023-06-08	Different construct Different mutation/modification 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 1–311（311 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	XOZ 1-[3,5-bis(fluoranyl)-4-[[3-(1,3-thiazol-5-yl)-1~{H}-pyrrolo[2,3-b]pyridin-4-yl]oxy]phenyl]-3-(2-methoxyethyl)urea × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；1.4 M NH4SO4, 0.3 M LiSO4, 0.1 M CAPS pH 9.8	Resolution 1.90 Å R-free 0.212
8PAV Crystal structure of MST1 with a MAP4K1 SMOL inhibitor Deposited 2023-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–311（311 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	XOZ 1-[3,5-bis(fluoranyl)-4-[[3-(1,3-thiazol-5-yl)-1~{H}-pyrrolo[2,3-b]pyridin-4-yl]oxy]phenyl]-3-(2-methoxyethyl)urea × 1 GOL GLYCEROL × 1 CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；1.4 M NH4SO4, 0.3 M LiSO4, 0.1 M CAPS pH 9.8	Resolution 1.90 Å R-free 0.212
8PAW Crystal structure of MST1 with a MAP4K1 SMOL inhibitor Deposited 2023-06-08	Different construct Different mutation/modification 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 1–311（311 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ASP ASPARTIC ACID × 1 XQL 1-[3,5-bis(fluoranyl)-4-[[3-(1-propan-2-ylpyrazol-3-yl)-1~{H}-pyrrolo[2,3-b]pyridin-4-yl]oxy]phenyl]-3-(2-methoxyethyl)urea × 1 GOL GLYCEROL × 1 CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；1.4 M NH4SO4, 0.3 M LiSO4, 0.1 M CAPS pH 9.8	Resolution 2.14 Å R-free 0.226
8PAW Crystal structure of MST1 with a MAP4K1 SMOL inhibitor Deposited 2023-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–311（311 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	XQL 1-[3,5-bis(fluoranyl)-4-[[3-(1-propan-2-ylpyrazol-3-yl)-1~{H}-pyrrolo[2,3-b]pyridin-4-yl]oxy]phenyl]-3-(2-methoxyethyl)urea × 1 GOL GLYCEROL × 1 CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；1.4 M NH4SO4, 0.3 M LiSO4, 0.1 M CAPS pH 9.8	Resolution 2.14 Å R-free 0.226
9IIC Crystal structure of HOIP RING2-LDD in complex with STK4 KD domain Deposited 2024-06-20	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 B 11–311（301 aa） Fragment：KD domain	Mutation：K59R	GOL GLYCEROL × 1 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；0.2 M Ammonium citrate tribasic (pH 7.0), 20% w/v Polyethylene glycol 3350	Resolution 2.78 Å R-free 0.280
9IIC Crystal structure of HOIP RING2-LDD in complex with STK4 KD domain Deposited 2024-06-20	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 A 11–311（301 aa） Fragment：KD domain	Mutation：K59R	GOL GLYCEROL × 1 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；0.2 M Ammonium citrate tribasic (pH 7.0), 20% w/v Polyethylene glycol 3350	Resolution 2.78 Å R-free 0.280
9VX3 Crystal structure of the peptide-bound form of HisMab-1 Fv-clasp Deposited 2025-07-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 432–480（49 aa） Chain B 432–480（49 aa）	Mutation：S37C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% (w/v) polyethylene glycol 3350, 0.1M HEPES (pH 7.0), 0.2M MgCl2	Resolution 2.39 Å R-free 0.237
9VX3 Crystal structure of the peptide-bound form of HisMab-1 Fv-clasp Deposited 2025-07-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 432–480（49 aa） Chain E 432–480（49 aa）	Mutation：S37C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% (w/v) polyethylene glycol 3350, 0.1M HEPES (pH 7.0), 0.2M MgCl2	Resolution 2.39 Å R-free 0.237

9 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	STK4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–282； UniProt 28–309 Author chain B； PDBConstruct 1–282； UniProt 28–309

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	8a5j
Deposition date deposition_date	2022-06-15
Structure title title	Crystal structure of Human STE20-like kinase 1, MST1 in complex with compound XMU-MP-1
Keywords keywords	serine-threonine kinase, autophosphorylation, MST1, TRANSFERASE; TRANSFERASE
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	25.87 Å
Radius of gyration Rg (electron density) rg_electron	24.68 Å
Forward intensity I(0) i0	59748400.00
Molecular weight molecular_weight	60601.0 kDa
Excluded volume excluded_volume	76162 Å³
Envelope volume envelope_volume	94275 Å³
Hydration-shell volume shell_volume	31266 Å³
Envelope diameter envelope_diameter	79.0 Å
Shell Rg shell_rg	32.45 Å
Envelope Rg envelope_rg	24.27 Å
Shape Rg shape_rg	24.68 Å
Total Rg total_rg	25.56 Å
Total atoms total_atoms	4247
Residues n_residues	524
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	76.3 Å
Rg (real space) rg_real	25.71 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	5.9750e+07
I(0) uncertainty (real space) i0_real_error	7.4640e+05
Rg (reciprocal space) rg_reciprocal	25.76 Å
I(0) (reciprocal space) i0_reciprocal	59750000.0000
Solution quality estimate total_estimate	0.9137
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	33.8 Å
Skewness Skewness skewness	0.101
Kurtosis Kurtosis kurtosis	-0.586
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12840000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.949

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Serine/threonine-protein kinase 4 37kDa subunit
Molecular weight formula_weight	32013.6 kDa
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	4369

EVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQ

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	4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide
Molecular weight formula_weight	416.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

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8. Citations (1)

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Unit-cell length a length_a	111.410 Å
Unit-cell length b length_b	111.410 Å
Unit-cell length c length_c	170.655 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	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.123 Å
Low-resolution limit resolution_low	93.290 Å
R factor r_factor	0.2430
R_work r_work	0.2427
R_free r_free	0.2482

fit	/app/data/saxs_computation/a5/8a5j/8a5j.fit
pddf	/app/data/pr_computation/a5/8a5j/8a5j.pr.out
profile	/app/data/saxs_computation/a5/8a5j/8a5j.dat

Crystal structure of Human STE20-like kinase 1, MST1 in complex with compound XMU-MP-1

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

Serine/threonine-protein kinase 4 37kDa subunit

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