4cfh

Structure of an active form of mammalian AMPK

Method: X-RAY DIFFRACTION Dmax: 102.0 Å Quality: REASONABLE

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

;5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 ;

RATTUS NORVEGICUS

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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 13–481 Chain C; UniProt 535–559 Fragment:RESIDUES 13-481 Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:RESIDUES 535-559 ;5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2 ; × 1 (O43741) ;5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1 ; × 1 (P80385) STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;CRYSTALS WERE GROWN BY THE HANGING DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 8% ISOPROPANOL AND 5% MPD AS PRECIPITANT IN 0.1M TRIS AT PH 7.5 AT 18 DEGREES. Resolution 3.24 Å R-free 0.268

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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAPK1_RAT
Isoform
PDB entities 1, 3
Chains and sequence ranges Author chain A; PDBConstruct 21–489; UniProt 13–481 Author chain C; PDBConstruct 3–27; UniProt 535–559

;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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 187–272 Fragment:RESIDUES 187-272 ;5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 ; × 1 (P54645) ;5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 ; × 1 (P54645) ;5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1 ; × 1 (P80385) STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;CRYSTALS WERE GROWN BY THE HANGING DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 8% ISOPROPANOL AND 5% MPD AS PRECIPITANT IN 0.1M TRIS AT PH 7.5 AT 18 DEGREES. Resolution 3.24 Å R-free 0.268

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 2–87; UniProt 187–272

;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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–330 Not recorded ;5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 ; × 1 (P54645) ;5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2 ; × 1 (O43741) ;5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 ; × 1 (P54645) STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;CRYSTALS WERE GROWN BY THE HANGING DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 8% ISOPROPANOL AND 5% MPD AS PRECIPITANT IN 0.1M TRIS AT PH 7.5 AT 18 DEGREES. Resolution 3.24 Å R-free 0.268

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 AAKG1_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; 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 4cfh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cfh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cfh
Deposition date deposition_date2013-11-18
Structure title titleStructure of an active form of mammalian AMPK
Keywords keywordsTRANSFERASE, TRANSFERASE PHOSPHORYLATION, ACTIVE FORM, NUCLEOTIDE-BINDING, STAUROSPORINE-BINDING, SERINE/THREONINE-PROTEIN KINASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.90
Radius of gyration Rg (electron density) rg_electron31.28
Forward intensity I(0) i0123388000.00
Molecular weight molecular_weight91203.0 kDa
Excluded volume excluded_volume115570 ų
Envelope volume envelope_volume148500 ų
Hydration-shell volume shell_volume39802 ų
Envelope diameter envelope_diameter110.0
Shell Rg shell_rg38.03
Envelope Rg envelope_rg31.09
Shape Rg shape_rg31.28
Total Rg total_rg31.91
Total atoms total_atoms6429
Residues n_residues792
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 dmax102.0
Rg (real space) rg_real31.89
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.2340e+08
I(0) uncertainty (real space) i0_real_error2.0880e+06
Rg (reciprocal space) rg_reciprocal31.90
I(0) (reciprocal space) i0_reciprocal123400000.0000
Solution quality estimate total_estimate0.6816
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.7
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43530000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.999; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)