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3fe3

Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant

Method: X-RAY DIFFRACTION Dmax: 105.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

MAP/microtubule affinity-regulating kinase 3

Homo sapiens

UniProt P27448

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 41–367 Chain B； UniProt 41–367 Fragment：CATALYTIC AND UBIQUITIN-ASSOCIATED DOMAINS, UNP residues 41-367 Mutation：T211A, S215A No other associated polymer 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

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 3FE3 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 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
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 41–367 Author chain B； PDBConstruct 2–328； UniProt 41–367

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3fe3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fe3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fe3
Deposition date deposition_date2008-11-27
Structure title titleCrystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant
Keywords keywords;SERINE/THREONINE PROTEIN KINASE; MARK;PAR-1; KIN1; UBA DOMAIN;C-TAK1;P78;MARK3, ATP-binding, Kinase, Nucleotide-binding, Phosphoprotein, Serine/threonine-protein kinase, Transferase ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier30.42 Å
Radius of gyration Rg (electron density) rg_electron29.60 Å
Forward intensity I(0) i079618400.00
Molecular weight molecular_weight72951.0 kDa
Excluded volume excluded_volume92556 ų
Envelope volume envelope_volume115700 ų
Hydration-shell volume shell_volume33348 ų
Envelope diameter envelope_diameter111.8 Å
Shell Rg shell_rg35.80 Å
Envelope Rg envelope_rg29.52 Å
Shape Rg shape_rg29.56 Å
Total Rg total_rg30.31 Å
Total atoms total_atoms5136
Residues n_residues634
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax105.0 Å
Rg (real space) rg_real30.49 Å
Rg uncertainty (real space) rg_real_error0.92 Å
I(0) (real space) i0_real7.9620e+07
I(0) uncertainty (real space) i0_real_error1.2950e+06
Rg (reciprocal space) rg_reciprocal30.46 Å
I(0) (reciprocal space) i0_reciprocal79620000.0000
Solution quality estimate total_estimate0.8655
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.3 Å
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.281
Angular range angular_range— – 0.2600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22420000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.878
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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) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3fe3a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.0 — automated matches
Domain ID domain_idd3fe3b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id3fe3A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3fe3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3fe3A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id3fe3B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id3fe3B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3fe3B03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
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8. Citations (3)

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9. Files and Curves (10)