SAXSdb — 4fzf

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

Calcium-binding protein 39

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 11–334	Fragment：Mo25-like, UNP residues 11-334	Serine/threonine-protein kinase MST4 × 1 （Q9P289） DKI 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 20% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.64 Å R-free 0.309

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 4FZF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1UPK Crystal structure of MO25 in complex with a C-terminal peptide of STRAD Deposited 2003-10-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–341（341 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；15% PEG 20000, 0.1 M MES PH 5.0, 3.3% W/V D-GLUCOSE MONOHYDRATE.	Resolution 1.85 Å R-free 0.230
1UPL Crystal structure of MO25 alpha Deposited 2003-10-07	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 1–341（341 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；15 % PEG 20000, 0.1 M MES PH 6.5, 4.4 % GAMMA BUTYROLACTONE	Resolution 2.60 Å R-free 0.280
1UPL Crystal structure of MO25 alpha Deposited 2003-10-07	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 1–341（341 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；15 % PEG 20000, 0.1 M MES PH 6.5, 4.4 % GAMMA BUTYROLACTONE	Resolution 2.60 Å R-free 0.280
2WTK Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex Deposited 2009-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 1–341（341 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PH 8.5	Resolution 2.65 Å R-free 0.291
2WTK Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex Deposited 2009-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–341（341 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PH 8.5	Resolution 2.65 Å R-free 0.291
3GNI Structure of STRAD and MO25 Deposited 2009-03-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–341（341 aa）	Not recorded	CIT CITRIC ACID × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.4；293 K；0.1 M MES pH 6.4, 10% PEG8000, 0.25 microL of 1 M NDSB-256, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.35 Å R-free 0.254
4FZA Crystal structure of MST4-MO25 complex Deposited 2012-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 11–334（324 aa） Fragment：Mo25-like, UNP residues 11-334	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 20% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.15 Å R-free 0.252
4FZD Crystal structure of MST4-MO25 complex with WSF motif Deposited 2012-07-06	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 11–334（324 aa） Fragment：Mo25-like, UNP residues 11-334	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 18% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.25 Å R-free 0.260
4NZW Crystal Structure of STK25-MO25 Complex Deposited 2013-12-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 8–334（327 aa） Fragment：UNP RESIDUES 8-334	Not recorded	J60 5-[(E)-(5-CHLORO-2-OXO-1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-N-[2-(DIETHYLAMINO)ETHYL]-2,4-DIMETHYL-1H-PYRROLE-3-CARBOXAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.1M HEPES PH 7.0, 1M SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K	Resolution 3.58 Å R-free 0.275
4O27 Crystal structure of MST3-MO25 complex with WIF motif Deposited 2013-12-16	Different construct 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 11–333（323 aa） Fragment：Mo25-like, UNP residues 11-333	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；0.1M Tris pH 8.5, 2.0M Ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 3.19 Å R-free 0.260
8VSU Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex Deposited 2024-01-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–341（341 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CAB39_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–328； UniProt 11–334

Serine/threonine-protein kinase MST4

Homo sapiens

UniProt Q9P289

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 18–297	Fragment：Kinase domain, UNP residues 18-297 Mutation：D162A	Calcium-binding protein 39 × 1 （Q9Y376） DKI 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 20% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.64 Å R-free 0.309

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 4FZF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3GGF Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin Deposited 2009-02-27	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 1–300（300 aa） Fragment：protein kinase	Not recorded	CD CADMIUM ION × 4 GVD [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-YL]ACETONITRILE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；12%w/v PEG 3350; 0.005M CdCl2; 0.1M HEPES, pH7.0 , VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.35 Å R-free 0.277
3GGF Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin Deposited 2009-02-27	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 1–300（300 aa） Fragment：protein kinase	Not recorded	CD CADMIUM ION × 3 GVD [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-YL]ACETONITRILE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；12%w/v PEG 3350; 0.005M CdCl2; 0.1M HEPES, pH7.0 , VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.35 Å R-free 0.277
3GGF Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin Deposited 2009-02-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–300（300 aa） Fragment：protein kinase Chain B 1–300（300 aa） Fragment：protein kinase	Not recorded	CD CADMIUM ION × 7 GVD [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-YL]ACETONITRILE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；12%w/v PEG 3350; 0.005M CdCl2; 0.1M HEPES, pH7.0 , VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.35 Å R-free 0.277
3W8I Crystal structure of CCM3 in complex with the C-terminal regulatory domain of MST4 Deposited 2013-03-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 346–416（71 aa） Fragment：UNP RESIDUES 346-416	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.1M Bis-Tris, 25% PEG3350, 0.3M ammonium acetate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.40 Å R-free 0.267
4FZA Crystal structure of MST4-MO25 complex Deposited 2012-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 18–297（280 aa） Fragment：Kinase domain, UNP residues 18-297	Mutation：D162A	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 20% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.15 Å R-free 0.252
4FZD Crystal structure of MST4-MO25 complex with WSF motif Deposited 2012-07-06	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 B 18–297（280 aa） Fragment：Kinase domain, UNP residues 18-297 Chain C 323–327（5 aa） Fragment：WSF motif, UNP residues 323-327	Mutation：D162A	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；0.1M Tris pH 8.0, 18% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.25 Å R-free 0.260
4GEH Crystal structure of MST4 dimerization domain complex with PDCD10 Deposited 2012-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 325–413（89 aa） Fragment：Dimerization domain, UNP residues 325-413	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.95 Å R-free 0.253
4GEH Crystal structure of MST4 dimerization domain complex with PDCD10 Deposited 2012-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 325–413（89 aa） Fragment：Dimerization domain, UNP residues 325-413	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.95 Å R-free 0.253
5XY9 Structure of the MST4 and 14-3-3 complex Deposited 2017-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 314–325（12 aa） Fragment：UNP residues 314-325 Chain D 314–325（12 aa） Fragment：UNP residues 314-325	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；0.2M MgCl2, 0.1M Tris pH 8.5, 25% PEG 3350	Resolution 2.30 Å R-free 0.245
5YF4 A kinase complex MST4-MOB4 Deposited 2017-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 320–335（16 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；0.1M HEPES, pH 7.5, 30% PEG 1000	Resolution 1.90 Å R-free 0.198
7B36 MST4 in complex with compound G-5555 Deposited 2020-11-28	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 1–300（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2 59T 8-[(trans-5-amino-1,3-dioxan-2-yl)methyl]-6-[2-chloro-4-(6-methylpyridin-2-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；solution: protein 12 mg/ml in buffer 25mM HEPES pH 7.5, 200 mM NaCl, 0.5mM TCEP, 5% glycerol reservoir: 28% PEG6000, 0.1M HEPES pH 7.5	Resolution 2.11 Å R-free 0.244
7B36 MST4 in complex with compound G-5555 Deposited 2020-11-28	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 C 1–300（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 59T 8-[(trans-5-amino-1,3-dioxan-2-yl)methyl]-6-[2-chloro-4-(6-methylpyridin-2-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；solution: protein 12 mg/ml in buffer 25mM HEPES pH 7.5, 200 mM NaCl, 0.5mM TCEP, 5% glycerol reservoir: 28% PEG6000, 0.1M HEPES pH 7.5	Resolution 2.11 Å R-free 0.244

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MST4_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 4–283； UniProt 18–297

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	4fzf
Deposition date deposition_date	2012-07-06
Structure title title	Crystal structure of MST4-MO25 complex with DKI
Keywords keywords	Scaffold protein, Protein Ser/Thr kinase, ATP binding, SIGNALING PROTEIN-TRANSFERASE-INHIBITOR complex; SIGNALING PROTEIN/TRANSFERASE/INHIBITOR
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	28.96 Å
Radius of gyration Rg (electron density) rg_electron	28.19 Å
Forward intensity I(0) i0	74434800.00
Molecular weight molecular_weight	69372.0 kDa
Excluded volume excluded_volume	87713 Å³
Envelope volume envelope_volume	113500 Å³
Hydration-shell volume shell_volume	33771 Å³
Envelope diameter envelope_diameter	97.5 Å
Shell Rg shell_rg	35.31 Å
Envelope Rg envelope_rg	28.00 Å
Shape Rg shape_rg	28.18 Å
Total Rg total_rg	28.99 Å
Total atoms total_atoms	4887
Residues n_residues	604
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	90.5 Å
Rg (real space) rg_real	28.88 Å
Rg uncertainty (real space) rg_real_error	0.54 Å
I(0) (real space) i0_real	7.4430e+07
I(0) uncertainty (real space) i0_real_error	1.0450e+06
Rg (reciprocal space) rg_reciprocal	28.91 Å
I(0) (reciprocal space) i0_reciprocal	74440000.0000
Solution quality estimate total_estimate	0.9068
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.5 Å
Skewness Skewness skewness	0.210
Kurtosis Kurtosis kurtosis	-0.513
Angular range angular_range	— – 0.2750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	19690000.0000
Real-space data points n_real_points	56
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.933

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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	Calcium-binding protein 39
Molecular weight formula_weight	38311.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4887

GAMASPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEKEPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYICTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQAKLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLK

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 polymer

Description description	Serine/threonine-protein kinase MST4
Molecular weight formula_weight	31930.7 kDa
EC 编号 ec_number	2.7.11.1
Mutation mutation	D162A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GAMADPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSSYVTKYYGSYLKGSKLWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLAAFGVAGQLTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFTKSFKEFIDACLNKDPSFRPTAKELLKHKFIVKNSKKTSYLTELIDRFKRWKAE

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 3 Entity 3 non-polymer

Description description	5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE
Molecular weight formula_weight	425.4 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	4fzfA01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily	10 — Leucine-rich Repeat Variant

Domain ID domain_id	4fzfB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

Domain ID domain_id	4fzfB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

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8. Citations (1)

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Unit-cell length a length_a	239.464 Å
Unit-cell length b length_b	239.464 Å
Unit-cell length c length_c	239.464 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	48

Space group space_group	I 4 3 2
Space-group number int_tables_number	211
Crystal system crystal_system	—

Resolution resolution	3.640 Å
Low-resolution limit resolution_low	38.850 Å
R factor r_factor	0.2551
R_work r_work	0.2521
R_free r_free	0.3092

fit	/app/data/saxs_computation/fz/4fzf/4fzf.fit
pddf	/app/data/pr_computation/fz/4fzf/4fzf.pr.out
profile	/app/data/saxs_computation/fz/4fzf/4fzf.dat

Crystal structure of MST4-MO25 complex with DKI

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

Calcium-binding protein 39

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase MST4

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)