2mrj

Structure of Fyn protein SH2 bound

Method: SOLUTION NMR Dmax: 42.1 Å Quality: EXCELLENT

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

Tyrosine-protein kinase Fyn

Homo sapiens

UniProt P06241

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 148–248 Fragment:UNP residues 149-248 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:1 mM [U-99% 13C; U-99% 15N] FynSH2 bound, 93% H2O/7% D2O | 93% H2O/7% 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.

50 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FYN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 12–112; UniProt 148–248

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 2mrj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mrj
Deposition date deposition_date2014-07-09
Structure title titleStructure of Fyn protein SH2 bound
Keywords keywordsFyn kinase, Src kinase, SH2 domain, TRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.72
Radius of gyration Rg (electron density) rg_electron13.21
Forward intensity I(0) i0633632000.00
Molecular weight molecular_weight210160.0 kDa
Excluded volume excluded_volume261850 ų
Envelope volume envelope_volume23082 ų
Hydration-shell volume shell_volume13402 ų
Envelope diameter envelope_diameter46.4
Shell Rg shell_rg20.45
Envelope Rg envelope_rg14.75
Shape Rg shape_rg13.17
Total Rg total_rg13.48
Total atoms total_atoms29430
Residues n_residues1800
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 dmax42.1
Rg (real space) rg_real13.63
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real6.3360e+08
I(0) uncertainty (real space) i0_real_error6.2050e+06
Rg (reciprocal space) rg_reciprocal13.64
I(0) (reciprocal space) i0_reciprocal633600000.0000
Solution quality estimate total_estimate0.9086
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.1
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha205300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2mrja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain

CATH v4.4 (1 domains)

Domain ID domain_id2mrjA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain

8. Citations (1)

9. Files and Curves (10)