SAXSdb — 2qnj

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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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 47–370 Chain B； UniProt 47–370	Not recorded	No other associated polymer	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

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 2QNJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3FE3 Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant Deposited 2008-11-27	Different construct Different mutation/modification 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 oligomeric state 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 oligomeric state 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 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 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 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 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 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 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 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 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 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 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 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
9VIR 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 Deposited 2025-06-18	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 48–370（323 aa）	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
9YR9 Structure of human MARK3 in complex with inhibitor Deposited 2025-10-16	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 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 oligomeric state 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 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 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 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 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 oligomeric state 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 oligomeric state 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 2–328； UniProt 47–370 Author chain B； PDBConstruct 2–328； UniProt 47–370

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2qnj
Deposition date deposition_date	2007-07-18
Structure title title	Kinase and Ubiquitin-associated domains of MARK3/Par-1
Keywords keywords	serine/threonine protein kinase, ubiquitin-associated domain, MARK, PAR-1, 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	32.95 Å
Radius of gyration Rg (electron density) rg_electron	32.62 Å
Forward intensity I(0) i0	77899000.00
Molecular weight molecular_weight	71405.0 kDa
Excluded volume excluded_volume	90051 Å³
Envelope volume envelope_volume	118380 Å³
Hydration-shell volume shell_volume	31944 Å³
Envelope diameter envelope_diameter	115.1 Å
Shell Rg shell_rg	37.21 Å
Envelope Rg envelope_rg	32.36 Å
Shape Rg shape_rg	32.59 Å
Total Rg total_rg	33.12 Å
Total atoms total_atoms	5028
Residues n_residues	640
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	108.1 Å
Rg (real space) rg_real	33.19 Å
Rg uncertainty (real space) rg_real_error	0.87 Å
I(0) (real space) i0_real	7.7900e+07
I(0) uncertainty (real space) i0_real_error	1.2510e+06
Rg (reciprocal space) rg_reciprocal	33.09 Å
I(0) (reciprocal space) i0_reciprocal	77890000.0000
Solution quality estimate total_estimate	0.8591
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.5 Å
Skewness Skewness skewness	0.439
Kurtosis Kurtosis kurtosis	-0.487
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	15290000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.684

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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) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2qnja1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.0 — automated matches

Domain ID domain_id	d2qnja2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2qnjb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.0 — automated matches

Domain ID domain_id	d2qnjb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id	2qnjA01
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	2qnjA02
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

Domain ID domain_id	2qnjA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	10 — Ubiquitin-associated (UBA) domain

Domain ID domain_id	2qnjB01
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	2qnjB02
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

Domain ID domain_id	2qnjB03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily	10 — Ubiquitin-associated (UBA) domain

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8. Citations (1)

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Unit-cell length a length_a	62.675 Å
Unit-cell length b length_b	112.544 Å
Unit-cell length c length_c	117.206 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2186
R_work r_work	0.2154
R_free r_free	0.2793

Description description	MAP/microtubule affinity-regulating kinase 3
Molecular weight formula_weight	37668.6 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5075

Kinase and Ubiquitin-associated domains of MARK3/Par-1

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 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 BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	47

fit	/app/data/saxs_computation/qn/2qnj/2qnj.fit
pddf	/app/data/pr_computation/qn/2qnj/2qnj.pr.out
profile	/app/data/saxs_computation/qn/2qnj/2qnj.dat