5ufu

Structure of AMPK bound to activator

Method: X-RAY DIFFRACTION Dmax: 121.6 Å Quality: GOOD

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

;5'-AMP-activated protein kinase catalytic subunit alpha-1 ;

Mus musculus

UniProt P54645

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 11–480 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-1 ; × 1 (P80386) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P80385) STU STAUROSPORINE × 1 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 1 CL CHLORIDE ION × 3 SO4 SULFATE ION × 2 AMP ADENOSINE MONOPHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 11–480 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-1 ; × 2 (P80386) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 2 (P80385) STU STAUROSPORINE × 2 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 2 CL CHLORIDE ION × 6 SO4 SULFATE ION × 4 AMP ADENOSINE MONOPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238

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.

20 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAPK1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–471; UniProt 11–480

;5'-AMP-activated protein kinase catalytic subunit alpha-1 ;

Mus musculus

UniProt Q5EG47

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 536–559 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-1 ; × 1 (P80386) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P80385) STU STAUROSPORINE × 1 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 1 CL CHLORIDE ION × 3 SO4 SULFATE ION × 2 AMP ADENOSINE MONOPHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 536–559 Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-1 ; × 2 (P80386) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 2 (P80385) STU STAUROSPORINE × 2 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 2 CL CHLORIDE ION × 6 SO4 SULFATE ION × 4 AMP ADENOSINE MONOPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name AAPK1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 480–503; UniProt 536–559

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

Rattus norvegicus

UniProt P80386

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 68–270 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (P54645,Q5EG47) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P80385) STU STAUROSPORINE × 1 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 1 CL CHLORIDE ION × 3 SO4 SULFATE ION × 2 AMP ADENOSINE MONOPHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 68–270 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 2 (P54645,Q5EG47) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 2 (P80385) STU STAUROSPORINE × 2 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 2 CL CHLORIDE ION × 6 SO4 SULFATE ION × 4 AMP ADENOSINE MONOPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238

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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAKB1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–204; UniProt 68–270

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

Rattus norvegicus

UniProt P80385

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–330 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (P54645,Q5EG47) ;5'-AMP-activated protein kinase subunit beta-1 ; × 1 (P80386) STU STAUROSPORINE × 1 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 1 CL CHLORIDE ION × 3 SO4 SULFATE ION × 2 AMP ADENOSINE MONOPHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–330 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 2 (P54645,Q5EG47) ;5'-AMP-activated protein kinase subunit beta-1 ; × 2 (P80386) STU STAUROSPORINE × 2 85V 1,4:3,6-dianhydro-2-O-(6-chloro-5-{4-[1-(hydroxymethyl)cyclopropyl]phenyl}-1H-benzimidazol-2-yl)-D-mannitol × 2 CL CHLORIDE ION × 6 SO4 SULFATE ION × 4 AMP ADENOSINE MONOPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;750 mM ammonium sulfate 500 mM lithium sulfate 100 mM trisodium citrate 1% ethylene glycol Resolution 3.45 Å R-free 0.238

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.

20 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAKG1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–330; UniProt 1–330

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 5ufu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ufu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ufu
Deposition date deposition_date2017-01-05
Structure title titleStructure of AMPK bound to activator
Keywords keywordsKinase, AMPK, activator, allostery, TRANSFERASE-ACTIVATOR complex; TRANSFERASE/ACTIVATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.10
Radius of gyration Rg (electron density) rg_electron34.85
Forward intensity I(0) i0119243000.00
Molecular weight molecular_weight86771.0 kDa
Excluded volume excluded_volume108030 ų
Envelope volume envelope_volume143820 ų
Hydration-shell volume shell_volume35776 ų
Envelope diameter envelope_diameter127.6
Shell Rg shell_rg39.47
Envelope Rg envelope_rg34.65
Shape Rg shape_rg34.90
Total Rg total_rg35.03
Total atoms total_atoms6125
Residues n_residues816
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 dmax121.6
Rg (real space) rg_real35.25
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.1920e+08
I(0) uncertainty (real space) i0_real_error2.1190e+06
Rg (reciprocal space) rg_reciprocal35.16
I(0) (reciprocal space) i0_reciprocal119200000.0000
Solution quality estimate total_estimate0.8511
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35370000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.854; Smooth: 0.775

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5ufuA01
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_id5ufuA02
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_id5ufuB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)