SAXSdb — 8s8o

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

cAMP-dependent protein kinase type II-alpha regulatory subunit

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–48 Chain B； UniProt 1–48	Fragment：N-terminal docking and dimerization domain, residues 1-52	Isoform 3 of Microtubule-associated protein 2 × 1 （P15146）	SOLUTION NMR NMR measurement conditions：pH 6.9；300.2 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition：0.5 mM [U-13C; U-15N] Microtubule associated protein 2c, 2 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 10 % v/v D2O, 17 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.56 mM Microtubule associated protein 2c, 1.12 mM [U-13C; U-15N] cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 10 % v/v D2O, 10 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.1 mM [U-15N] Microtubule associated protein 2c, 0.4 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 8 % v/v D2O, 40 mg/mL Pf1 phage, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.23 mM [U-15N] Microtubule associated protein 2c, 0.92 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 7.5 % v/v D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.45 mM I,V-13C; I,L,V-15N Microtubule associated protein 2c, 1.8 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 7.5 % v/v D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 8S8O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2IZX Molecular Basis of AKAP Specificity for PKA Regulatory Subunits Deposited 2006-07-27	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 A 3–43（41 aa） Fragment：3-43 Chain B 3–43（41 aa） Fragment：3-43	Not recorded	DTD DITHIANE DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1 M TRI-SODIUM CITRATE, 0.1 M TRIS-HCL PH 7.5	Resolution 1.30 Å R-free 0.194
2KYG Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to AML1-ETO activity Deposited 2010-05-25	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–45（45 aa） Chain B 1–45（45 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；303 K；Ionic strength (raw mmCIF value) 0.0；Pressure ambient NMR sample composition 2 mM [U-99% 13C; U-99% 15N] NHR3, 2 mM [U-99% 13C; U-99% 15N] PKA(RIIa), 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	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 A 2–44（43 aa） Chain B 2–44（43 aa）	Not recorded	CD CADMIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 2–44（43 aa） Chain D 2–44（43 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 2–44（43 aa） Chain F 2–44（43 aa）	Not recorded	CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 2–44（43 aa） Chain H 2–44（43 aa）	Not recorded	CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 2–44（43 aa） Chain J 2–44（43 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
4ZP3 AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of regulatory subunits of PKA Deposited 2015-05-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 2–44（43 aa） Chain L 2–44（43 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG3350, Cadmium chloride, Sodium acetate	Resolution 2.63 Å R-free 0.268
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain B 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain D 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain F 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain H 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain J 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H77 Crystal structure of the PKA-protein A fusion protein Deposited 2016-11-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain K 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268 Chain L 5–41（37 aa） Fragment：UNP RESIDUES 5-41,UNP RESIDUES 220-268	Mutation：G222A, G240A Mutation：G222A, G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.5；296 K；0.1M sodium acetate pH 4.5, 0.68M sodium citrate pH 4.5	Resolution 3.20 Å R-free 0.284
5H78 Crystal structure of the PKA-DHR14 fusion protein Deposited 2016-11-17	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 5–41（37 aa） Fragment：RESIDUES 4-40 (UNP RESIDUES 5-41),RESIDUES 41-196 Chain B 5–41（37 aa） Fragment：RESIDUES 4-40 (UNP RESIDUES 5-41),RESIDUES 41-196	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；296 K；0.05M sodium cacodylate pH 6.5, 0.01M magnesium chloride, 0.2M potassium chloride, 12%(w/v) PEG 4000	Resolution 2.00 Å R-free 0.207
5XBY Crystal structure of the PKA-Protein A fusion protein (end-to-end fusion) Deposited 2017-03-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 5–44（40 aa） Fragment：UNP RESIDUES 5-44,UNP RESIDUES 217-269 Chain B 5–44（40 aa） Fragment：UNP RESIDUES 5-44,UNP RESIDUES 217-269	Mutation：G240A Mutation：G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；296 K；100mM Tris pH 8.5, 2.16M Sodium formate	Resolution 3.25 Å R-free 0.307
5XBY Crystal structure of the PKA-Protein A fusion protein (end-to-end fusion) Deposited 2017-03-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 5–44（40 aa） Fragment：UNP RESIDUES 5-44,UNP RESIDUES 217-269 Chain D 5–44（40 aa） Fragment：UNP RESIDUES 5-44,UNP RESIDUES 217-269	Mutation：G240A Mutation：G240A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；296 K；100mM Tris pH 8.5, 2.16M Sodium formate	Resolution 3.25 Å R-free 0.307
9NXN Crystal structure of CN:RII alpha Deposited 2025-03-25	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 44–103（60 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；289 K；0.1 M sodium citrate pH 5.0, 0.1 M Magnesium chloride hexahydrate, 15% PEG 4000	Resolution 2.10 Å R-free 0.250

7 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KAP2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–52； UniProt 1–48 Author chain B； PDBConstruct 5–52； UniProt 1–48

Isoform 3 of Microtubule-associated protein 2

Rattus norvegicus

UniProt P15146

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 C； UniProt 84–111	Fragment：N-terminal PKA binding region, residues 80-120	cAMP-dependent protein kinase type II-alpha regulatory subunit × 2 （P13861）	SOLUTION NMR NMR measurement conditions：pH 6.9；300.2 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition：0.5 mM [U-13C; U-15N] Microtubule associated protein 2c, 2 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 10 % v/v D2O, 17 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.56 mM Microtubule associated protein 2c, 1.12 mM [U-13C; U-15N] cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 10 % v/v D2O, 10 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.1 mM [U-15N] Microtubule associated protein 2c, 0.4 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 8 % v/v D2O, 40 mg/mL Pf1 phage, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.23 mM [U-15N] Microtubule associated protein 2c, 0.92 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 7.5 % v/v D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：0.45 mM I,V-13C; I,L,V-15N Microtubule associated protein 2c, 1.8 mM cAMP-dependent protein kinase type II-alpha regulatory subunit, 50 mM MOPS, 100 mM sodium chloride, 7.5 % v/v D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 8S8O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9FUM Dimeric 14-3-3 zeta in complex with MAP2c peptide containing pS435 Deposited 2024-06-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 432–439（8 aa） Chain F 432–439（8 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CD CADMIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；100 mM HEPES pH(7.5), 400 mM Sodium acetate, 8mM Cadmium sulfate	Resolution 2.45 Å R-free 0.275
9FVL Dimeric 14-3-3 zeta in complex with unphosphorylated MAP2c peptide Deposited 2024-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 333–362（30 aa） Chain F 333–362（30 aa）	Not recorded	CD CADMIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；100 mM HEPES pH(7.5), 400 mM Sodium acetate, 8mM Cadmium sulfate	Resolution 2.08 Å R-free 0.283

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

View Construct and Data Evidence

UniProt name	MTAP2_RAT
Isoform	P15146-3
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–28； UniProt 84–111

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	8s8o
Deposition date deposition_date	2024-03-06
最后修订 last_revision	2024-09-25
Structure title title	Solution Structure of cAMP-dependent Protein Kinase RII-alpha Subunit Dimerization and Docking Domain Complex with Microtubule Associated Protein 2c (84-111)
Keywords keywords	AKAP, PKA, MAP2c, IDP, protein-protein complex, 4-helix bundle, microtubule, PROTEIN BINDING; PROTEIN BINDING
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.32 Å
Radius of gyration Rg (electron density) rg_electron	15.55 Å
Forward intensity I(0) i0	1156600000.00
Molecular weight molecular_weight	290470.0 kDa
Excluded volume excluded_volume	364720 Å³
Envelope volume envelope_volume	44243 Å³
Hydration-shell volume shell_volume	19093 Å³
Envelope diameter envelope_diameter	67.3 Å
Shell Rg shell_rg	26.10 Å
Envelope Rg envelope_rg	20.48 Å
Shape Rg shape_rg	15.45 Å
Total Rg total_rg	16.09 Å
Total atoms total_atoms	41000
Residues n_residues	2640
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	57.4 Å
Rg (real space) rg_real	16.31 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	1.1570e+09
I(0) uncertainty (real space) i0_real_error	1.4000e+07
Rg (reciprocal space) rg_reciprocal	16.32 Å
I(0) (reciprocal space) i0_reciprocal	1157000000.0000
Solution quality estimate total_estimate	0.7811
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.4 Å
Skewness Skewness skewness	0.326
Kurtosis Kurtosis kurtosis	-0.218
Angular range angular_range	— – 0.4900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	480500.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.727; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	cAMP-dependent protein kinase type II-alpha regulatory subunit
Molecular weight formula_weight	5789.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	41000

GAMGMSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPAS

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 BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Isoform 3 of Microtubule-associated protein 2
Molecular weight formula_weight	3015.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

RETAEEVSARIVQVVTAEAVAVLKGEQE

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli BL21(DE3)

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8. Citations (1)

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fit	/app/data/saxs_computation/s8/8s8o/8s8o.fit
pddf	/app/data/pr_computation/s8/8s8o/8s8o.pr.out
profile	/app/data/saxs_computation/s8/8s8o/8s8o.dat

Solution Structure of cAMP-dependent Protein Kinase RII-alpha Subunit Dimerization and Docking Domain Complex with Microtubule Associated Protein 2c (84-111)

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

cAMP-dependent protein kinase type II-alpha regulatory subunit

State in the Current Structure

Other States of the Same Protein in the Database

Isoform 3 of Microtubule-associated protein 2

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)