6b2e

Structure of full length human AMPK (a2b2g1) in complex with a small molecule activator SC4.

Method: X-RAY DIFFRACTION Dmax: 123.0 Å Quality: GOOD

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

;5'-AMP-activated protein kinase catalytic subunit alpha-2 ;

Homo sapiens

UniProt P54646

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–552 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 STU STAUROSPORINE × 1 CG7 5-{[6-chloro-5-(2'-hydroxy[1,1'-biphenyl]-4-yl)-1H-imidazo[4,5-b]pyridin-2-yl]oxy}-2-methylbenzoic acid × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;6-8% PEG 3350, 0.1 M MgCl2, 0.001% cocamidopropyl betaine and 0.1 M imidazole Resolution 3.80 Å R-free 0.277

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.

14 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAPK2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–565; UniProt 2–552

;5'-AMP-activated protein kinase subunit beta-2 ;

Homo sapiens

UniProt O43741

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–272 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase catalytic subunit alpha-2 ; × 1 (P54646) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 STU STAUROSPORINE × 1 CG7 5-{[6-chloro-5-(2'-hydroxy[1,1'-biphenyl]-4-yl)-1H-imidazo[4,5-b]pyridin-2-yl]oxy}-2-methylbenzoic acid × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;6-8% PEG 3350, 0.1 M MgCl2, 0.001% cocamidopropyl betaine and 0.1 M imidazole Resolution 3.80 Å R-free 0.277

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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAKB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–272; UniProt 1–272

;5'-AMP-activated protein kinase subunit gamma-1 ;

Homo sapiens

UniProt P54619

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 2–331 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-2 ; × 1 (P54646) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) Cycloheptakis-(1-4)-(alpha-D-glucopyranose) × 1 STU STAUROSPORINE × 1 CG7 5-{[6-chloro-5-(2'-hydroxy[1,1'-biphenyl]-4-yl)-1H-imidazo[4,5-b]pyridin-2-yl]oxy}-2-methylbenzoic acid × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;6-8% PEG 3350, 0.1 M MgCl2, 0.001% cocamidopropyl betaine and 0.1 M imidazole Resolution 3.80 Å R-free 0.277

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.

22 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAKG1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 7–336; UniProt 2–331

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 6b2e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b2e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b2e
Deposition date deposition_date2017-09-19
Structure title titleStructure of full length human AMPK (a2b2g1) in complex with a small molecule activator SC4.
Keywords keywordsPhosphorylated, Active, Heterotrimer, Kinase., TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.86
Radius of gyration Rg (electron density) rg_electron34.43
Forward intensity I(0) i0143845000.00
Molecular weight molecular_weight95117.0 kDa
Excluded volume excluded_volume118520 ų
Envelope volume envelope_volume166440 ų
Hydration-shell volume shell_volume41855 ų
Envelope diameter envelope_diameter131.3
Shell Rg shell_rg39.37
Envelope Rg envelope_rg34.09
Shape Rg shape_rg34.45
Total Rg total_rg34.77
Total atoms total_atoms6720
Residues n_residues929
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax123.0
Rg (real space) rg_real35.00
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real1.4380e+08
I(0) uncertainty (real space) i0_real_error2.6070e+06
Rg (reciprocal space) rg_reciprocal34.92
I(0) (reciprocal space) i0_reciprocal143800000.0000
Solution quality estimate total_estimate0.8527
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.495
Kurtosis Kurtosis kurtosis-0.009
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44910000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.771; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.828

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6b2eA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)