4jsn

structure of mTORdeltaN-mLST8 complex

Method: X-RAY DIFFRACTION Dmax: 169.3 Å Quality: GOOD

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

Serine/threonine-protein kinase mTOR

Homo sapiens

UniProt P42345

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1376–2549 Fragment:FAT FRB KINASE Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris, pH 8.5, 6-8% PEG 8000, 500 mM NaCl, 10 % (v/v) Glycerol, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1376–2549 Fragment:FAT FRB KINASE Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris, pH 8.5, 6-8% PEG 8000, 500 mM NaCl, 10 % (v/v) Glycerol, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.256

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.

66 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTOR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1174; UniProt 1376–2549 Author chain B; PDBConstruct 1–1174; UniProt 1376–2549

Target of rapamycin complex subunit LST8

Homo sapiens

UniProt Q9BVC4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris, pH 8.5, 6-8% PEG 8000, 500 mM NaCl, 10 % (v/v) Glycerol, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris, pH 8.5, 6-8% PEG 8000, 500 mM NaCl, 10 % (v/v) Glycerol, 10 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.256

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.

44 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LST8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–326; UniProt 1–326 Author chain D; PDBConstruct 1–326; UniProt 1–326

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 4jsn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4jsn
Deposition date deposition_date2013-03-22
Structure title titlestructure of mTORdeltaN-mLST8 complex
Keywords keywordshelical repeat, kinase, wd40 repeat, protein kinase, Raptor, transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier52.49
Radius of gyration Rg (electron density) rg_electron52.04
Forward intensity I(0) i01448610000.00
Molecular weight molecular_weight314630.0 kDa
Excluded volume excluded_volume392500 ų
Envelope volume envelope_volume586960 ų
Hydration-shell volume shell_volume92497 ų
Envelope diameter envelope_diameter172.8
Shell Rg shell_rg57.05
Envelope Rg envelope_rg50.49
Shape Rg shape_rg52.04
Total Rg total_rg52.21
Total atoms total_atoms22097
Residues n_residues2746
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 dmax169.3
Rg (real space) rg_real52.35
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real1.4490e+09
I(0) uncertainty (real space) i0_real_error2.8440e+07
Rg (reciprocal space) rg_reciprocal52.58
I(0) (reciprocal space) i0_reciprocal1449000000.0000
Solution quality estimate total_estimate0.8280
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.7
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.532
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76370000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4jsnC01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id4jsnD01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)