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2wtk

Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex

Method: X-RAY DIFFRACTION Dmax: 154.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CALCIUM-BINDING PROTEIN 39

HOMO SAPIENS

UniProt Q9Y376

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain D； UniProt 1–341 Not recorded STE20-RELATED KINASE ADAPTER PROTEIN ALPHA × 1 （Q7RTN6） SERINE/THREONINE-PROTEIN KINASE 11 × 1 （Q15831） 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 1–341 Not recorded STE20-RELATED KINASE ADAPTER PROTEIN ALPHA × 1 （Q7RTN6） SERINE/THREONINE-PROTEIN KINASE 11 × 1 （Q15831） 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

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 2WTK 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 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 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 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 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
3GNI Structure of STRAD and MO25 Deposited 2009-03-17 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 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 construct 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 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 construct 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
4FZF Crystal structure of MST4-MO25 complex with DKI Deposited 2012-07-06 Different construct 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 11–334（324 aa） Fragment：Mo25-like, UNP residues 11-334
Not recorded 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
4NZW Crystal Structure of STK25-MO25 Complex Deposited 2013-12-13 Different construct 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 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 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 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 10 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 1–341； UniProt 1–341 Author chain D； PDBConstruct 1–341； UniProt 1–341

STE20-RELATED KINASE ADAPTER PROTEIN ALPHA

HOMO SAPIENS

UniProt Q7RTN6

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain E； UniProt 59–431 Fragment：PSEUDOKINASE DOMAIN, RESIDUES 59-431 CALCIUM-BINDING PROTEIN 39 × 1 （Q9Y376） SERINE/THREONINE-PROTEIN KINASE 11 × 1 （Q15831） 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain B； UniProt 59–431 Fragment：PSEUDOKINASE DOMAIN, RESIDUES 59-431 CALCIUM-BINDING PROTEIN 39 × 1 （Q9Y376） SERINE/THREONINE-PROTEIN KINASE 11 × 1 （Q15831） 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

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 2WTK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3GNI Structure of STRAD and MO25 Deposited 2009-03-17 Different construct 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 59–431（373 aa） Fragment：Protein kinase domain
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
8VSU Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex Deposited 2024-01-24 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–394（394 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

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STRAA_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–373； UniProt 59–431 Author chain E； PDBConstruct 1–373； UniProt 59–431

SERINE/THREONINE-PROTEIN KINASE 11

HOMO SAPIENS

UniProt Q15831

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain F； UniProt 43–347 Fragment：KINASE DOMAIN, RESIDUES 43-347 Mutation：YES CALCIUM-BINDING PROTEIN 39 × 1 （Q9Y376） STE20-RELATED KINASE ADAPTER PROTEIN ALPHA × 1 （Q7RTN6） 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain C； UniProt 43–347 Fragment：KINASE DOMAIN, RESIDUES 43-347 Mutation：YES CALCIUM-BINDING PROTEIN 39 × 1 （Q9Y376） STE20-RELATED KINASE ADAPTER PROTEIN ALPHA × 1 （Q7RTN6） 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

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 2WTK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4ZDR Crystal structure of 14-3-3[zeta]-LKB1 fusion protein Deposited 2015-04-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 333–340（8 aa） Fragment：UNP residues 1-230,UNP residues 333-340
Chain B 333–340（8 aa） Fragment：UNP residues 1-230,UNP residues 333-340
Mutation：T240E Mutation：T240E GOL GLYCEROL × 3 SO4 SULFATE ION × 2 TME PROPANE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；289 K；1.4 M Li2SO4, 0.1 M BIS-TRIS propane
Resolution 2.90 Å R-free 0.245
5WXN Structure of the LKB1 and 14-3-3 complex Deposited 2017-01-08 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 331–343（13 aa） Fragment：UNP residues 331-343
Chain D 331–343（13 aa） Fragment：UNP residues 331-343
Non-standard monomer：Yes (specific site not provided by mmCIF) 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；289 K；0.15 M ammonium chloride, 18% PEG3350
Resolution 2.93 Å R-free 0.254
8VSU Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex Deposited 2024-01-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–433（433 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

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STK11_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C； PDBConstruct 1–305； UniProt 43–347 Author chain F； PDBConstruct 1–305； UniProt 43–347

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 2wtk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wtk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wtk
Deposition date deposition_date2009-09-16
Structure title titleStructure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex
Keywords keywords;TRANSFERASE-METAL-BINDING PROTEIN COMPLEX, TRANSFERASE METAL-BINDING PROTEIN COMPLEX, KINASE, NUCLEUS, SERINE/THREONINE-PROTEIN KINASE, PSEUDOKINASE, PHOSPHOPROTEIN, SIGNAL TRANSDUCTION, TRANSFERASE, NUCLEOTIDE-BINDING ;; TRANSFERASE/METAL-BINDING PROTEIN
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_guinier45.47 Å
Radius of gyration Rg (electron density) rg_electron45.60 Å
Forward intensity I(0) i0617390000.00
Molecular weight molecular_weight209690.0 kDa
Excluded volume excluded_volume264410 ų
Envelope volume envelope_volume370920 ų
Hydration-shell volume shell_volume68414 ų
Envelope diameter envelope_diameter159.6 Å
Shell Rg shell_rg49.71 Å
Envelope Rg envelope_rg44.79 Å
Shape Rg shape_rg45.61 Å
Total Rg total_rg45.73 Å
Total atoms total_atoms14748
Residues n_residues1818
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 dmax154.1 Å
Rg (real space) rg_real45.67 Å
Rg uncertainty (real space) rg_real_error1.71 Å
I(0) (real space) i0_real6.1740e+08
I(0) uncertainty (real space) i0_real_error1.2670e+07
Rg (reciprocal space) rg_reciprocal45.47 Å
I(0) (reciprocal space) i0_reciprocal617200000.0000
Solution quality estimate total_estimate0.8500
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.0 Å
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.520
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81210000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.833
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2wtka_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.15 — Mo25 protein
Domain ID domain_idd2wtkc1
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_idd2wtkd_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.15 — Mo25 protein
Domain ID domain_idd2wtkf1
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 (10 domains)

Domain ID domain_id2wtkA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2wtkB01
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_id2wtkB02
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_id2wtkC01
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_id2wtkC02
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_id2wtkD01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id2wtkE01
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_id2wtkE02
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_id2wtkF01
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_id2wtkF02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
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8. Citations (1)

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9. Files and Curves (10)