9zbk

mTORC2 in complex with Akt1

Method: ELECTRON MICROSCOPY Dmax: 229.7 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 80–2549 Not recorded Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Rapamycin-insensitive companion of mTOR × 1 (Q6R327) Target of rapamycin complex 2 subunit MAPKAP1 × 1 (Q9BPZ7) RAC-alpha serine/threonine-protein kinase × 1 (P31749) ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

66 other PDB entries and 84 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 1–2470; UniProt 80–2549

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 7–324 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Rapamycin-insensitive companion of mTOR × 1 (Q6R327) Target of rapamycin complex 2 subunit MAPKAP1 × 1 (Q9BPZ7) RAC-alpha serine/threonine-protein kinase × 1 (P31749) ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

44 other PDB entries and 52 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 B; PDBConstruct 1–318; UniProt 7–324

Rapamycin-insensitive companion of mTOR

Homo sapiens

UniProt Q6R327

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 25–1694 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Target of rapamycin complex 2 subunit MAPKAP1 × 1 (Q9BPZ7) RAC-alpha serine/threonine-protein kinase × 1 (P31749) ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RICTR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–1670; UniProt 25–1694

Target of rapamycin complex 2 subunit MAPKAP1

Homo sapiens

UniProt Q9BPZ7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–268 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Rapamycin-insensitive companion of mTOR × 1 (Q6R327) RAC-alpha serine/threonine-protein kinase × 1 (P31749) ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIN1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–269; UniProt 1–268

RAC-alpha serine/threonine-protein kinase

Homo sapiens

UniProt P31749

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 141–478 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Rapamycin-insensitive companion of mTOR × 1 (Q6R327) Target of rapamycin complex 2 subunit MAPKAP1 × 1 (Q9BPZ7) ZN ZINC ION × 1 A1AID (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

37 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AKT1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–338; UniProt 141–478

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 9zbk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zbk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zbk
Deposition date deposition_date2025-11-20
Structure title titlemTORC2 in complex with Akt1
Keywords keywordscellular growth control, TRANSFERASE, Torin; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.08
Radius of gyration Rg (electron density) rg_electron64.74
Forward intensity I(0) i05412330000.00
Molecular weight molecular_weight404750.0 kDa
Excluded volume excluded_volume388520 ų
Envelope volume envelope_volume983030 ų
Hydration-shell volume shell_volume125840 ų
Envelope diameter envelope_diameter224.2
Shell Rg shell_rg66.16
Envelope Rg envelope_rg63.47
Shape Rg shape_rg64.73
Total Rg total_rg64.78
Total atoms total_atoms30622
Residues n_residues4149
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 dmax229.7
Rg (real space) rg_real65.05
Rg uncertainty (real space) rg_real_error2.33
I(0) (real space) i0_real5.4130e+09
I(0) uncertainty (real space) i0_real_error1.1810e+08
Rg (reciprocal space) rg_reciprocal65.07
I(0) (reciprocal space) i0_reciprocal5412000000.0000
Solution quality estimate total_estimate0.8672
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.6
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha139700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)