SAXSdb — 2kyg

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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 1–45 Chain B； UniProt 1–45	Not recorded	Protein CBFA2T1 × 1 （Q06455）	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

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 2KYG	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
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
8S8O Solution Structure of cAMP-dependent Protein Kinase RII-alpha Subunit Dimerization and Docking Domain Complex with Microtubule Associated Protein 2c (84-111) Deposited 2024-03-06	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–48（48 aa） Fragment：N-terminal docking and dimerization domain, residues 1-52 Chain B 1–48（48 aa） Fragment：N-terminal docking and dimerization domain, residues 1-52	Not recorded	No recorded non-water small molecule	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
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 6–50； UniProt 1–45 Author chain B； PDBConstruct 6–50； UniProt 1–45

Protein CBFA2T1

Homo sapiens

UniProt Q06455

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 437–467	Not recorded	cAMP-dependent protein kinase type II-alpha regulatory subunit × 2 （P13861）	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

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 2KYG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WQ6 The tetramer structure of the nervy homolgy two (NHR2) domain of AML1-ETO is critical for AML1-ETO'S activity Deposited 2004-09-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 335–403（69 aa） Fragment：NHR2 domain Chain B 335–403（69 aa） Fragment：NHR2 domain	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；pH 5.6；293 K；100mM Na citrate (pH 5.6), 100mM MgCl2, 30% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.00 Å R-free 0.270
2DJ8 Solution Structure of zf-MYND Domain of Protein CBFA2TI (Protein MTG8) Deposited 2006-03-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 449–450（2 aa） Fragment：zf-MYND	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition 0.95mM zf-MYND domain, U-13C, 15N; 20mM d-Tris_HCl (pH 7.0); 100mM NaCl; 1mM d-DTT, 0.02% NaN3; 0.05mM ZnCl2; 1mM IDA; 90% H2O, 10% D20 \| 90% H2O, 10% D20	Resolution not provided
2KNH The Solution structure of the eTAFH domain of AML1-ETO complexed with HEB peptide Deposited 2009-08-25	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 119–216（98 aa） Fragment：eTAFH domain (UNP residues 119-216)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 350；Pressure ambient NMR sample composition 25 mM Bis-Tris, 1 mM EDTA, 350 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2OD1 Solution structure of the MYND domain from human AML1-ETO Deposited 2006-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 510–559（50 aa） Fragment：MYND domain	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Pressure 1 NMR sample composition 1-2mM protein, 25mM Bis-Tris, 5mM DTT, 50uM ZnCl2, 95% H20, 5% D2O \| 95% H20, 5% D2O	Resolution not provided
2ODD Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor Deposited 2006-12-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 510–559（50 aa） Fragment：MYND domain (AML1-ETO, residues 658-707)	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Pressure 1 NMR sample composition 2mM SMRT-MYND, 25mM Bis-Tris, pH 6.8, 50uM ZnCl2, 1mM DTT, 95%H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
2PP4 Solution Structure of ETO-TAFH refined in explicit solvent Deposited 2007-04-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 119–225（107 aa） Fragment：TAFH domain, residues 119-225	Mutation：F136Y	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；293 K；Pressure ambient NMR sample composition 1.1 mM protein, 200 mM phosphate buffer, 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
4JOL Complex structure of AML1-ETO NHR2 domain with HEB fragment Deposited 2013-03-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400) Chain C 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 mM Tris, 20% ETHANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.91 Å R-free 0.252
4JOL Complex structure of AML1-ETO NHR2 domain with HEB fragment Deposited 2013-03-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400) Chain D 338–400（63 aa） Fragment：NHR2 domain of AML1-ETO (unp residues 338-400)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 mM Tris, 20% ETHANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.91 Å R-free 0.252

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MTG8_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 8–38； UniProt 437–467

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	2kyg
Deposition date deposition_date	2010-05-25
Structure title title	Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to AML1-ETO activity
Keywords keywords	protein/protein, homodimer bound to monomer, 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	17.23 Å
Radius of gyration Rg (electron density) rg_electron	16.19 Å
Forward intensity I(0) i0	752937000.00
Molecular weight molecular_weight	231100.0 kDa
Excluded volume excluded_volume	289470 Å³
Envelope volume envelope_volume	63217 Å³
Hydration-shell volume shell_volume	24039 Å³
Envelope diameter envelope_diameter	78.7 Å
Shell Rg shell_rg	29.07 Å
Envelope Rg envelope_rg	22.43 Å
Shape Rg shape_rg	16.07 Å
Total Rg total_rg	16.98 Å
Total atoms total_atoms	32505
Residues n_residues	2070
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	52.6 Å
Rg (real space) rg_real	17.26 Å
Rg uncertainty (real space) rg_real_error	0.10 Å
I(0) (real space) i0_real	7.3560e+08
I(0) uncertainty (real space) i0_real_error	6.5390e+06
Rg (reciprocal space) rg_reciprocal	17.23 Å
I(0) (reciprocal space) i0_reciprocal	752900000.0000
Solution quality estimate total_estimate	0.6829
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	19.4 Å
Skewness Skewness skewness	0.317
Kurtosis Kurtosis kurtosis	-0.312
Angular range angular_range	— – 0.4600 Å⁻¹
Current regularization parameter α current_alpha	9.2080
Highest regularization parameter α highest_alpha	759100.0000
Real-space data points n_real_points	77
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.958; Stabil: 0.930; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.232

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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	5621.4 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	32505

GAMGSMSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARA

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	Protein CBFA2T1
Molecular weight formula_weight	4184.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

AMADIGSASGYVPEEIWKKAEEAVNEVKRQAMTELQKA

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

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2kyga1
Class class	a — All alpha proteins
Fold Fold fold	a.31 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Superfamily Superfamily superfamily	a.31.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Family Family family	a.31.1.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit

Domain ID domain_id	d2kyga2
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	d2kygb1
Class class	a — All alpha proteins
Fold Fold fold	a.31 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Superfamily Superfamily superfamily	a.31.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Family Family family	a.31.1.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit

Domain ID domain_id	d2kygb2
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 (2 domains)

Domain ID domain_id	2kygA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	890 — cAMP-dependent Protein Kinase, Chain A
Homologous superfamily homologous superfamily	10 — cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain

Domain ID domain_id	2kygB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	890 — cAMP-dependent Protein Kinase, Chain A
Homologous superfamily homologous superfamily	10 — cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain

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8. Citations (1)

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fit	/app/data/saxs_computation/ky/2kyg/2kyg.fit
pddf	/app/data/pr_computation/ky/2kyg/2kyg.pr.out
profile	/app/data/saxs_computation/ky/2kyg/2kyg.dat

Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to AML1-ETO activity

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

Protein CBFA2T1

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

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)