2dn7

Solution structures of the 6th fn3 domain of human receptor-type tyrosine-protein phosphatase F

Method: SOLUTION NMR Dmax: 43.6 Å Quality: REASONABLE

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

Receptor-type tyrosine-protein phosphatase F

Homo sapiens

UniProt P10586

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 811–904 Fragment:Fibronectin type III domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1mM fn3 domain U-15N,13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 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.

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTPRF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–101; UniProt 811–904

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 2dn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2dn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2dn7
Deposition date deposition_date2006-04-25
Structure title titleSolution structures of the 6th fn3 domain of human receptor-type tyrosine-protein phosphatase F
Keywords keywords;LAR protein, Leukocyte antigen related, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SIGNALING PROTEIN, HYDROLASE ;; SIGNALING PROTEIN, HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.45
Radius of gyration Rg (electron density) rg_electron15.96
Forward intensity I(0) i0822542000.00
Molecular weight molecular_weight232980.0 kDa
Excluded volume excluded_volume287520 ų
Envelope volume envelope_volume36429 ų
Hydration-shell volume shell_volume15440 ų
Envelope diameter envelope_diameter84.2
Shell Rg shell_rg26.84
Envelope Rg envelope_rg23.80
Shape Rg shape_rg15.92
Total Rg total_rg16.33
Total atoms total_atoms32340
Residues n_residues2140
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 dmax43.6
Rg (real space) rg_real15.16
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real7.7850e+08
I(0) uncertainty (real space) i0_real_error6.5040e+06
Rg (reciprocal space) rg_reciprocal16.76
I(0) (reciprocal space) i0_reciprocal822500000.0000
Solution quality estimate total_estimate0.6838
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.8
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha3.7840
Highest regularization parameter α highest_alpha277700.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.021; Oscil: 0.980; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2dn7a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd2dn7a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2dn7a3
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_id2dn7A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)