2npu

The solution structure of the rapamycin-binding domain of mTOR (FRB)

Method: SOLUTION NMR Dmax: 47.2 Å Quality: GOOD

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

FKBP12-rapamycin complex-associated protein

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2015–2114 Fragment:FRB No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100mM;Pressure ambient NMR sample composition:0.1 mM FRB domain U-15N,13C; '25mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.1 mM FRB domain U-15N; 25mM phosphate buffer, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.1 mM FRB domain U-15N,13C with unlabelled aromatics; 25mM phosphate buffer, 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.

66 other PDB entries and 84 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FRAP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 27–126; UniProt 2015–2114

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 2npu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2npu
Deposition date deposition_date2006-10-30
Structure title titleThe solution structure of the rapamycin-binding domain of mTOR (FRB)
Keywords keywordsFour-helix bundle, Transferase; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.70
Radius of gyration Rg (electron density) rg_electron13.76
Forward intensity I(0) i02125660000.00
Molecular weight molecular_weight391140.0 kDa
Excluded volume excluded_volume487920 ų
Envelope volume envelope_volume31295 ų
Hydration-shell volume shell_volume15916 ų
Envelope diameter envelope_diameter54.9
Shell Rg shell_rg22.59
Envelope Rg envelope_rg16.95
Shape Rg shape_rg13.69
Total Rg total_rg14.12
Total atoms total_atoms54080
Residues n_residues3232
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 dmax47.2
Rg (real space) rg_real13.63
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.1260e+09
I(0) uncertainty (real space) i0_real_error2.4270e+07
Rg (reciprocal space) rg_reciprocal13.64
I(0) (reciprocal space) i0_reciprocal2126000000.0000
Solution quality estimate total_estimate0.8551
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha200100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.711; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2npua1
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.7 — FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)
Family Family familya.24.7.1 — FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)
Domain ID domain_idd2npua2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2npuA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily150 — FKBP12-rapamycin binding domain

8. Citations (1)

9. Files and Curves (10)