7jhh

Cryo-EM structure of ATP-bound fully inactive AMPK in complex with Fab and nanobody

Method: ELECTRON MICROSCOPY Dmax: 148.0 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 Other combination Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 22–480 Chain A; UniProt 535–559 Fragment:UNP residues 22-480,535-559 ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) Maltodextrin-binding protein × 1 (C3SHQ8) Fab light chain × 1 Fab heavy chain × 1 Nanobody × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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 1–459; UniProt 22–480 Author chain A; PDBConstruct 460–484; 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 Other combination Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 75–272 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit gamma-1 ; × 1 (P54619) Maltodextrin-binding protein × 1 (C3SHQ8) Fab light chain × 1 Fab heavy chain × 1 Nanobody × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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 1–198; UniProt 75–272

;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 × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 24–327 Not recorded ;5'-AMP-activated protein kinase catalytic subunit alpha-1 ; × 1 (Q13131) ;5'-AMP-activated protein kinase subunit beta-2 ; × 1 (O43741) Maltodextrin-binding protein × 1 (C3SHQ8) Fab light chain × 1 Fab heavy chain × 1 Nanobody × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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 G; PDBConstruct 3–306; UniProt 24–327

Maltodextrin-binding protein

Escherichia coli K-12

UniProt C3SHQ8

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 × 7 其他Polymer 1 PDB declaration: heptameric(7) 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) Fab light chain × 1 Fab heavy chain × 1 Nanobody × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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.

15 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SHQ8_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 2–368; UniProt 26–392

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 7jhh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7jhh
Deposition date deposition_date2020-07-20
Structure title titleCryo-EM structure of ATP-bound fully inactive AMPK in complex with Fab and nanobody
Keywords keywordsAMPK, ATP, fully inactive, KD-displaced, TRANSFERASE-IMMUNE SYSTEM complex; TRANSFERASE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.46
Radius of gyration Rg (electron density) rg_electron46.16
Forward intensity I(0) i0516016000.00
Molecular weight molecular_weight190410.0 kDa
Excluded volume excluded_volume239540 ų
Envelope volume envelope_volume353450 ų
Hydration-shell volume shell_volume64131 ų
Envelope diameter envelope_diameter155.2
Shell Rg shell_rg50.35
Envelope Rg envelope_rg45.14
Shape Rg shape_rg46.14
Total Rg total_rg46.40
Total atoms total_atoms13418
Residues n_residues1698
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 dmax148.0
Rg (real space) rg_real46.40
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real5.1600e+08
I(0) uncertainty (real space) i0_real_error8.8480e+06
Rg (reciprocal space) rg_reciprocal46.46
I(0) (reciprocal space) i0_reciprocal516000000.0000
Solution quality estimate total_estimate0.6562
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.0
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha48590000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 0.021; Positv: 1.000; Valcen: 1.000; Smooth: 0.623

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7jhhH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7jhhH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7jhhL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7jhhL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)