2ltu

Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit

Method: SOLUTION NMR Dmax: 34.4 Å Quality: REASONABLE

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

;5'-AMP-activated protein kinase catalytic subunit alpha-2 ;

Homo sapiens

UniProt P54646

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 282–339 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 50;Pressure ambient NMR sample composition:0.2 mM [U-100% 13C; U-100% 15N] AID protein, 50 mM sodium phosphate, 10 % [U-100% 2H] D2O, 90 % H2O, 1 mM EDTA, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AAPK2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–62; UniProt 282–339

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 2ltu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ltu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ltu
Deposition date deposition_date2012-06-01
Structure title titleSolution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit
Keywords keywordsAMPK, AID, TRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.11
Radius of gyration Rg (electron density) rg_electron12.64
Forward intensity I(0) i0330178000.00
Molecular weight molecular_weight140230.0 kDa
Excluded volume excluded_volume170070 ų
Envelope volume envelope_volume30066 ų
Hydration-shell volume shell_volume14829 ų
Envelope diameter envelope_diameter62.5
Shell Rg shell_rg23.33
Envelope Rg envelope_rg18.48
Shape Rg shape_rg12.61
Total Rg total_rg13.05
Total atoms total_atoms18860
Residues n_residues1240
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 dmax34.4
Rg (real space) rg_real12.40
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real3.1580e+08
I(0) uncertainty (real space) i0_real_error2.2740e+06
Rg (reciprocal space) rg_reciprocal13.19
I(0) (reciprocal space) i0_reciprocal330200000.0000
Solution quality estimate total_estimate0.6874
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.2
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.8850
Highest regularization parameter α highest_alpha77840.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.996; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2ltuA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain

8. Citations (1)

9. Files and Curves (10)