9kp4

Crystal structure of human CASTOR1 in apo form

Method: X-RAY DIFFRACTION Dmax: 186.3 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Cytosolic arginine sensor for mTORC1 subunit 1

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 NH4 AMMONIUM ION × 2 ACY ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Barium chloride, 30% v/v ethanol, 0.2 M NH4Ac, 0.1 M Tris pH 8.5, and 25% PEG 3350. Resolution 3.08 Å R-free 0.264
2 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 27–392 Chain D; UniProt 27–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 NH4 AMMONIUM ION × 2 ACY ACETIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Barium chloride, 30% v/v ethanol, 0.2 M NH4Ac, 0.1 M Tris pH 8.5, and 25% PEG 3350. Resolution 3.08 Å R-free 0.264

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.

366 other PDB entries and 490 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392 Author chain B; PDBConstruct 2–367; UniProt 27–392 Author chain C; PDBConstruct 2–367; UniProt 27–392 Author chain D; PDBConstruct 2–367; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,Cytosolic arginine sensor for mTORC1 subunit 1

Homo sapiens

UniProt Q8WTX7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–329 Chain B; UniProt 1–329 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 NH4 AMMONIUM ION × 2 ACY ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Barium chloride, 30% v/v ethanol, 0.2 M NH4Ac, 0.1 M Tris pH 8.5, and 25% PEG 3350. Resolution 3.08 Å R-free 0.264
2 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–329 Chain D; UniProt 1–329 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 NH4 AMMONIUM ION × 2 ACY ACETIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Barium chloride, 30% v/v ethanol, 0.2 M NH4Ac, 0.1 M Tris pH 8.5, and 25% PEG 3350. Resolution 3.08 Å R-free 0.264

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.

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAST1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 376–704; UniProt 1–329 Author chain B; PDBConstruct 376–704; UniProt 1–329 Author chain C; PDBConstruct 376–704; UniProt 1–329 Author chain D; PDBConstruct 376–704; UniProt 1–329

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 9kp4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kp4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9kp4
Deposition date deposition_date2024-11-22
最后修订 last_revision2026-03-25
Structure title titleCrystal structure of human CASTOR1 in apo form
Keywords keywordsCASTOR1, mTORC1, arginine sensor, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.40
Radius of gyration Rg (electron density) rg_electron56.11
Forward intensity I(0) i0942107000.00
Molecular weight molecular_weight265400.0 kDa
Excluded volume excluded_volume335680 ų
Envelope volume envelope_volume507150 ų
Hydration-shell volume shell_volume80252 ų
Envelope diameter envelope_diameter185.9
Shell Rg shell_rg53.53
Envelope Rg envelope_rg53.87
Shape Rg shape_rg56.11
Total Rg total_rg55.99
Total atoms total_atoms18780
Residues n_residues2457
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 dmax186.3
Rg (real space) rg_real56.46
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real9.4210e+08
I(0) uncertainty (real space) i0_real_error1.7730e+07
Rg (reciprocal space) rg_reciprocal56.33
I(0) (reciprocal space) i0_reciprocal941900000.0000
Solution quality estimate total_estimate0.8562
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31120000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.393

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)