6c9j

AMP-activated protein kinase bound to pharmacological activator R734

Method: X-RAY DIFFRACTION Dmax: 121.7 Å Quality: REASONABLE

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

;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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 22–480 Chain A; UniProt 535–559 Mutation:S108D Non-standard monomer:Yes (specific site not provided by mmCIF) ;5'-AMP-activated protein kinase subunit beta-1 ; × 1 (Q9Y478) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M tri-ammonium citrate pH7, 12% w/v PEG 3350 Resolution 3.05 Å R-free 0.225

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 1
Chains and sequence ranges Author chain A; PDBConstruct 11–469; UniProt 22–480 Author chain A; PDBConstruct 470–494; UniProt 535–559

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

Homo sapiens

UniProt Q9Y478

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 B; UniProt 68–270 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M tri-ammonium citrate pH7, 12% w/v PEG 3350 Resolution 3.05 Å R-free 0.225

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.

11 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAKB1_HUMAN
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 ;

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–325 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit beta-1 ; × 1 (Q9Y478) R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M tri-ammonium citrate pH7, 12% w/v PEG 3350 Resolution 3.05 Å R-free 0.225

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 1–325; UniProt 1–325

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 6c9j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c9j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c9j
Deposition date deposition_date2018-01-26
Structure title titleAMP-activated protein kinase bound to pharmacological activator R734
Keywords keywordsAMPK, activator, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.32
Radius of gyration Rg (electron density) rg_electron34.97
Forward intensity I(0) i0142880000.00
Molecular weight molecular_weight99736.0 kDa
Excluded volume excluded_volume126570 ų
Envelope volume envelope_volume163660 ų
Hydration-shell volume shell_volume40162 ų
Envelope diameter envelope_diameter130.4
Shell Rg shell_rg39.95
Envelope Rg envelope_rg34.79
Shape Rg shape_rg35.01
Total Rg total_rg35.24
Total atoms total_atoms7034
Residues n_residues859
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 dmax121.7
Rg (real space) rg_real35.44
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real1.4290e+08
I(0) uncertainty (real space) i0_real_error2.3740e+06
Rg (reciprocal space) rg_reciprocal35.37
I(0) (reciprocal space) i0_reciprocal142900000.0000
Solution quality estimate total_estimate0.6461
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.2
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51170000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.921; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6c9jc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.37 — CBS-domain pair
Superfamily Superfamily superfamilyd.37.1 — CBS-domain pair
Family Family familyd.37.1.1 — CBS-domain pair
Domain ID domain_idd6c9jc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.37 — CBS-domain pair
Superfamily Superfamily superfamilyd.37.1 — CBS-domain pair
Family Family familyd.37.1.1 — CBS-domain pair

CATH v4.4 (2 domains)

Domain ID domain_id6c9jA01
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_id6c9jA02
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)