2l5s

Solution structure of the extracellular domain of the TGF-beta type I receptor

Method: SOLUTION NMR Dmax: 41.5 Å Quality: GOOD

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

TGF-beta receptor type-1

Homo sapiens

UniProt P36897

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 31–115 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.2;300 K;Ionic strength (raw mmCIF value) 0.025;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] TbRI-1, 95% H2O/5% D2O | 95% H2O/5% 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.

44 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–87; UniProt 31–115

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 2l5s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l5s
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2l5s
Deposition date deposition_date2010-11-04
Structure title titleSolution structure of the extracellular domain of the TGF-beta type I receptor
Keywords keywordsALK5, transforming growth factor beta, type I receptor, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.55
Radius of gyration Rg (electron density) rg_electron12.69
Forward intensity I(0) i0144960000.00
Molecular weight molecular_weight94618.0 kDa
Excluded volume excluded_volume115980 ų
Envelope volume envelope_volume19549 ų
Hydration-shell volume shell_volume11924 ų
Envelope diameter envelope_diameter48.8
Shell Rg shell_rg19.64
Envelope Rg envelope_rg14.44
Shape Rg shape_rg12.71
Total Rg total_rg12.87
Total atoms total_atoms12840
Residues n_residues870
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 dmax41.5
Rg (real space) rg_real12.54
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.4500e+08
I(0) uncertainty (real space) i0_real_error1.6780e+06
Rg (reciprocal space) rg_reciprocal12.54
I(0) (reciprocal space) i0_reciprocal145000000.0000
Solution quality estimate total_estimate0.8174
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.7
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha115200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; 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_id2l5sA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)