SAXSdb — 9vir

▼

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

MAP/microtubule affinity-regulating kinase 3

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 48–370	Mutation：I62L/L72R/V116I/G137K/F141Y/A146E	A1ESF ~{N}-[5-[[4-[[(3~{R},3~{a}~{R},6~{a}~{S})-3-methoxy-2,3,3~{a},6~{a}-tetrahydrofuro[3,2-b]furan-6-yl]oxy]-5-chloranyl-pyrimidin-2-yl]amino]-2-[[(2~{R},8~{R})-2-fluoranyl-1,2,3,5,6,7-hexahydropyrrolizin-8-yl]methoxy]phenyl]-1-methyl-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 6.5；293.15 K；0.1M MES pH 6.5, 25% PEG 8000 and 0.2M (NH4)2SO4	Resolution 2.80 Å R-free 0.316

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 9VIR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2QNJ Kinase and Ubiquitin-associated domains of MARK3/Par-1 Deposited 2007-07-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 47–370（324 aa） Chain B 47–370（324 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5M LiSO4, 100 mM HEPES pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.70 Å R-free 0.279
3FE3 Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant Deposited 2008-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 41–367（327 aa） Fragment：CATALYTIC AND UBIQUITIN-ASSOCIATED DOMAINS, UNP residues 41-367 Chain B 41–367（327 aa） Fragment：CATALYTIC AND UBIQUITIN-ASSOCIATED DOMAINS, UNP residues 41-367	Mutation：T211A, S215A Mutation：T211A, S215A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；100mM Hepes, 200mM calcium chloride, 15-18% PEG 3350, 5mM DTT , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.233
7P1L The MARK3 Kinase Domain Bound To AA-CS-1-008 Deposited 2021-07-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–366（319 aa）	Not recorded	V5E 5-Bromo-4-N-[2-(1H-imidazol-5-yl)ethyl]-2-N-[3-(morpholin-4-ylmethyl)phenyl]pyrimidine-2,4-diamine × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium formate pH 7.0 24% PEG3350	Resolution 1.95 Å R-free 0.242
7P1L The MARK3 Kinase Domain Bound To AA-CS-1-008 Deposited 2021-07-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 48–366（319 aa）	Not recorded	V5E 5-Bromo-4-N-[2-(1H-imidazol-5-yl)ethyl]-2-N-[3-(morpholin-4-ylmethyl)phenyl]pyrimidine-2,4-diamine × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M sodium formate pH 7.0 24% PEG3350	Resolution 1.95 Å R-free 0.242
8UOH Crystal structure of human NUAK1-MARK3 kinase domain chimera bound with small molecule inhibitor #10 Deposited 2023-10-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 48–370（323 aa） Chain B 48–370（323 aa）	Mutation：I61L, V116I, G137K, F141Y, A146E, L72R Mutation：I61L, V116I, G137K, F141Y, A146E, L72R	EDO 1,2-ETHANEDIOL × 9 NI NICKEL (II) ION × 1 X4W (6P)-6-[(4S)-imidazo[1,2-a]pyridin-3-yl]-4-[(1R)-1-phenylethyl]-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.1；287 K；8.09 mg/mL Tray302895 fine screen F2: 0.1M HEPES pH 7.1, 0.2M MgCl, 8 (%v/v) PEG 8000; protein buffer contains: 20 mM HEPES pH 7.5, 100 mM NaCl, 5 mM BME	Resolution 2.15 Å R-free 0.220
8UOI Crystal structure of human NUAK1-MARK3 kinase domain chimera bound with small molecule inhibitor #65 Deposited 2023-10-19	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–370（323 aa）	Mutation：I62L, V116I, G137K, F141Y, A146E, L72/71R, V205K	X3Q (7M)-7-[(4S)-imidazo[1,2-b]pyridazin-3-yl]-1-[(1R)-1-phenylethyl]-3-(piperazin-1-yl)pyrido[3,4-b]pyrazin-2(1H)-one × 1 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.86；293 K；CID102002 (MARK3-NUAK chimera V205K), PID7361-1, 8.0 mg/ml. Tray 314126g7; JCSG_B4 screen: 9.0% (w/V) PEG 8000, 8% (V/V) ethylene glycol, 100mM HEPES free acid / sodium hydroxide pH 7.86; 2,5mM BSI109151 / UCB1705233; crystal back soaked over night with 2.5mM UCB1816405; cryo: 25% EG in soak; puck itc9-6	Resolution 1.80 Å R-free 0.198
8UOJ Crystal structure of human NUAK1-MARK3 kinase domain chimera bound with azepane (R)-#50 small molecule inhibitor Deposited 2023-10-19	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–370（323 aa）	Mutation：I62L, V116I, G137K, F141Y, A146E, L72R Non-standard monomer：Yes (specific site not provided by mmCIF)	X5I (6M)-4-{[(2R)-azepan-2-yl]methyl}-6-[(4R)-imidazo[1,2-a]pyridin-3-yl]-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one × 1 EDO 1,2-ETHANEDIOL × 5 CL CHLORIDE ION × 1 BEZ BENZOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；100mM Tris base / HCl pH 7.5, 200mM Magnesium chloride, 10% (w/V) PEG8000; 2.5mM UCB1718758 (bsi109321)	Resolution 1.60 Å R-free 0.186
8UOK Crystal structure of human NUAK1-MARK3 (7 mutations) kinase domain chimera bound with small molecule inhibitor #31 Deposited 2023-10-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 48–370（323 aa） Chain B 48–370（323 aa）	Mutation：I62L, V116I, G137K, F141Y, A146E, L72/71R, V205K Mutation：I62L, V116I, G137K, F141Y, A146E, L72/71R, V205K	X5N (6P)-6-[(4R)-imidazo[1,2-a]pyridin-3-yl]-4-(piperidin-4-yl)-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one × 2 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；318327A2 (JCSG E10 FS), 100mM Bicine, pH 8.3, PEG 6000 10.6 %w/v with 2.5mM compound, 25% EG	Resolution 1.85 Å R-free 0.192
8UOL Crystal structure of human NUAK1-MARK3 (6 mutations) kinase domain chimera bound with small molecule inhibitor #31 Deposited 2023-10-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 48–370（323 aa） Chain B 48–370（323 aa）	Mutation：I62L, V116I, G137K, F141Y, A146E, L72/71R Mutation：I62L, V116I, G137K, F141Y, A146E, L72/71R	X4H Narazaciclib × 2 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；JCSG E12 condition: 0.1 M Imidazole pH 8.0, 10 (%v/v) PEG 8000, 2.5mM compound 31)	Resolution 1.90 Å R-free 0.211
9VFO Crystal Structure of the NUAK1-MARK3 kinase domain chimera bound with small molecule inhibitor 2-amino-N-(5-((5-chloro-4-(((3R,3aR,6R,6aR)-6-methoxyhexahydrofuro[3,2-b]furan-3-yl)oxy)pyrimidin-2-yl)amino)-2-((2-(dimethylamino)ethyl)(methyl)amino)phenyl)acetamide Deposited 2025-06-11	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–370（323 aa）	Not recorded	A1ER0 N-[5-[[4-[[(3R,3aR,6R,6aR)-3-methoxy-2,3,3a,5,6,6a-hexahydrofuro[3,2-b]furan-6-yl]oxy]-5-chloranyl-pyrimidin-2-yl]amino]-2-[2-(dimethylamino)ethyl-methyl-amino]phenyl]-2-azanyl-ethanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293.15 K；0.1M MES pH 6.5, 25% PEG 8000 and 0.2M (NH4)2SO4	Resolution 2.50 Å R-free 0.237
9VGR Crystal Structure of the NUAK1-MARK3 kinase domain chimera bound with small molecule inhibitor 4-((5-((5-chloro-4-(((3R,3aR,6R,6aR)-6-methoxyhexahydrofuro[3,2-b]furan-3-yl)oxy)pyrimidin-2-yl)amino)-2-((2-(dimethylamino)ethyl)(methyl)amino)phenyl)carbamoyl)-1-methyl-3H-pyrazol-1-ium-3-ide Deposited 2025-06-14	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–370（323 aa）	Not recorded	A1ER9 N-[5-[[4-[[(3R,3aR,6R,6aR)-3-methoxy-2,3,3a,5,6,6a-hexahydrofuro[3,2-b]furan-6-yl]oxy]-5-chloranyl-pyrimidin-2-yl]amino]-2-[2-(dimethylamino)ethyl-methyl-amino]phenyl]-1-methyl-pyrazole-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293.15 K；0.1M MES pH 6.5, 25% PEG 8000 and 0.2M (NH4)2SO4	Resolution 2.00 Å R-free 0.197
9YR9 Structure of human MARK3 in complex with inhibitor Deposited 2025-10-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–367（320 aa） Fragment：residues 48-367	Not recorded	A1CZY 3-({5-chloro-2-[2-(difluoromethoxy)-4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl}amino)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1M HEPES pH 7.0, 0.1M ammonium sulphate, 25% PEG3350	Resolution 2.40 Å R-free 0.253
9YR9 Structure of human MARK3 in complex with inhibitor Deposited 2025-10-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 48–367（320 aa） Fragment：residues 48-367	Not recorded	A1CZY 3-({5-chloro-2-[2-(difluoromethoxy)-4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl}amino)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1M HEPES pH 7.0, 0.1M ammonium sulphate, 25% PEG3350	Resolution 2.40 Å R-free 0.253
9YSQ Structure of a human NUAK1-MARK3 kinase domain chimera in complex with inhibitor Deposited 2025-10-19	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–370（323 aa）	Mutation：I62L, L72R, V116I, G137K, F141Y, A146E	A1CZY 3-({5-chloro-2-[2-(difluoromethoxy)-4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl}amino)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1M HEPES pH 7.0, 0.2M magnesium formate, 17% PEG3350	Resolution 2.40 Å R-free 0.248
9YSQ Structure of a human NUAK1-MARK3 kinase domain chimera in complex with inhibitor Deposited 2025-10-19	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 48–370（323 aa）	Mutation：I62L, L72R, V116I, G137K, F141Y, A146E	A1CZY 3-({5-chloro-2-[2-(difluoromethoxy)-4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl}amino)thiophene-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1M HEPES pH 7.0, 0.2M magnesium formate, 17% PEG3350	Resolution 2.40 Å R-free 0.248
9ZZW Structure of human MARK3 in complex with inhibitor Deposited 2026-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 48–367（320 aa） Fragment：residues 48-367	Not recorded	A1C86 2-({5-chloro-2-[4-(4-ethylpiperazin-1-yl)-2-methoxyanilino]pyrimidin-4-yl}amino)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；25%PEG 3350, 0.1M (NH4)2SO4, and 0.1M MES pH 6.0	Resolution 2.76 Å R-free 0.286
9ZZW Structure of human MARK3 in complex with inhibitor Deposited 2026-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 48–367（320 aa） Fragment：residues 48-367	Not recorded	A1C86 2-({5-chloro-2-[4-(4-ethylpiperazin-1-yl)-2-methoxyanilino]pyrimidin-4-yl}amino)benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；25%PEG 3350, 0.1M (NH4)2SO4, and 0.1M MES pH 6.0	Resolution 2.76 Å R-free 0.286

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

View Construct and Data Evidence

UniProt name	MARK3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–326； UniProt 48–370

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9vir
Deposition date deposition_date	2025-06-18
最后修订 last_revision	2026-04-22
Structure title title	Crystal Structure of the NUAK1-MARK3 kinase domain chimera bound with small molecule inhibitor N-(5-((5-chloro-4-(((3aS,6R,6aR)-6-methoxy-3a,5,6,6a-tetrahydrofuro[3,2-b]furan-3-yl)oxy)pyrimidin-2-yl)amino)-2-(((2R,7aR)-2-fluorotetrahydro-1H-pyrrolizin-7a(5H)-yl)methoxy)phenyl)-1-methyl-1H-pyrazole-4-carboxamide
Keywords keywords	protein kinase, complex, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	28.41 Å
Radius of gyration Rg (electron density) rg_electron	28.23 Å
Forward intensity I(0) i0	67839800.00
Molecular weight molecular_weight	42627.0 kDa
Excluded volume excluded_volume	41006 Å³
Envelope volume envelope_volume	82575 Å³
Hydration-shell volume shell_volume	26140 Å³
Envelope diameter envelope_diameter	108.1 Å
Shell Rg shell_rg	32.75 Å
Envelope Rg envelope_rg	30.28 Å
Shape Rg shape_rg	28.22 Å
Total Rg total_rg	28.62 Å
Total atoms total_atoms	3232
Residues n_residues	443
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	101.5 Å
Rg (real space) rg_real	28.96 Å
Rg uncertainty (real space) rg_real_error	0.91 Å
I(0) (real space) i0_real	6.7840e+07
I(0) uncertainty (real space) i0_real_error	1.0230e+06
Rg (reciprocal space) rg_reciprocal	28.79 Å
I(0) (reciprocal space) i0_reciprocal	67830000.0000
Solution quality estimate total_estimate	0.7725
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	0.741
Kurtosis Kurtosis kurtosis	0.024
Angular range angular_range	— – 0.2800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	9454000.0000
Real-space data points n_real_points	57
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.546; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.531; Smooth: 0.870

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	MAP/microtubule affinity-regulating kinase 3
Molecular weight formula_weight	37744.7 kDa
EC 编号 ec_number	2.7.11.1
Mutation mutation	I62L/L72R/V116I/G137K/F141Y/A146E
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	3232

MGSDEQPHIGNYRLLKTLGKGNFAKVKRARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIIKLFEVIETEKTLYLIMEYASKGEVYDYLVEHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSSE

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	MAP/microtubule affinity-regulating kinase 3
Molecular weight formula_weight	27762.1 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

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	;~{N}-[5-[[4-[[(3~{R},3~{a}~{R},6~{a}~{S})-3-methoxy-2,3,3~{a},6~{a}-tetrahydrofuro[3,2-b]furan-6-yl]oxy]-5-chloranyl-pyrimidin-2-yl]amino]-2-[[(2~{R},8~{R})-2-fluoranyl-1,2,3,5,6,7-hexahydropyrrolizin-8-yl]methoxy]phenyl]-1-methyl-pyrazole-4-carboxamide ;
Molecular weight formula_weight	642.1 kDa
Source method src_method	man
Copy count entity_count	1

▶

8. Citations (1)

▶

Unit-cell length a length_a	84.360 Å
Unit-cell length b length_b	45.320 Å
Unit-cell length c length_c	165.677 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.30 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	46.314 Å
R factor r_factor	0.2694
R_work r_work	0.2672
R_free r_free	0.3158

fit	/app/data/saxs_computation/vi/9vir/9vir.fit
pddf	/app/data/pr_computation/vi/9vir/9vir.pr.out
profile	/app/data/saxs_computation/vi/9vir/9vir.dat

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

MAP/microtubule affinity-regulating kinase 3

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

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)