7jij

ATP-bound AMP-activated protein kinase

Method: X-RAY DIFFRACTION Dmax: 141.8 Å Quality: GOOD

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

Maltose/maltodextrin ABC transporter substrate-binding protein MalE

Escherichia coli

UniProt A0A6D0N546

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 × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 26–392 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M tri-lithium citrate,10% w/v PEG3350, pH7.5,0.01 M barium chloride Resolution 5.50 Å R-free 0.323

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6D0N546_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain M; PDBConstruct 2–368; UniProt 26–392

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

Homo sapiens

UniProt Q13131

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 × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 22–559 Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose/maltodextrin ABC transporter substrate-binding protein MalE × 1 (A0A6D0N546) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M tri-lithium citrate,10% w/v PEG3350, pH7.5,0.01 M barium chloride Resolution 5.50 Å R-free 0.323

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAPK1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–484; UniProt 22–559

;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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 76–272 Not recorded Maltose/maltodextrin ABC transporter substrate-binding protein MalE × 1 (A0A6D0N546) ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M tri-lithium citrate,10% w/v PEG3350, pH7.5,0.01 M barium chloride Resolution 5.50 Å R-free 0.323

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 3
Chains and sequence ranges Author chain B; PDBConstruct 2–198; UniProt 76–272

;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 × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 24–327 Not recorded Maltose/maltodextrin ABC transporter substrate-binding protein MalE × 1 (A0A6D0N546) ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M tri-lithium citrate,10% w/v PEG3350, pH7.5,0.01 M barium chloride Resolution 5.50 Å R-free 0.323

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 4
Chains and sequence ranges Author chain G; PDBConstruct 3–306; UniProt 24–327

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 7jij

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jij
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jij
Deposition date deposition_date2020-07-23
Structure title titleATP-bound AMP-activated protein kinase
Keywords keywordsAMPK, activation, ATP-binding, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.71
Radius of gyration Rg (electron density) rg_electron41.75
Forward intensity I(0) i0251448000.00
Molecular weight molecular_weight132950.0 kDa
Excluded volume excluded_volume168110 ų
Envelope volume envelope_volume247890 ų
Hydration-shell volume shell_volume50747 ų
Envelope diameter envelope_diameter146.6
Shell Rg shell_rg45.43
Envelope Rg envelope_rg40.86
Shape Rg shape_rg41.77
Total Rg total_rg41.90
Total atoms total_atoms9372
Residues n_residues1160
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 dmax141.8
Rg (real space) rg_real41.87
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real2.5140e+08
I(0) uncertainty (real space) i0_real_error4.5400e+06
Rg (reciprocal space) rg_reciprocal41.71
I(0) (reciprocal space) i0_reciprocal251400000.0000
Solution quality estimate total_estimate0.8671
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.391
Kurtosis Kurtosis kurtosis-0.504
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97280000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.816

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)