1ayd

CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE

Method: X-RAY DIFFRACTION Dmax: 43.6 Å Quality: GOOD

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

PROTEIN-TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN)

Mus musculus

UniProt P35235

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 4–103 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN11_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–101; UniProt 4–103

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 1ayd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ayd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ayd
Deposition date deposition_date1994-05-15
Structure title titleCRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE
Keywords keywordsHYDROLASE(SH2 DOMAIN); HYDROLASE(SH2 DOMAIN)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.05
Radius of gyration Rg (electron density) rg_electron12.54
Forward intensity I(0) i02548070.00
Molecular weight molecular_weight11051.0 kDa
Excluded volume excluded_volume13818 ų
Envelope volume envelope_volume14967 ų
Hydration-shell volume shell_volume10300 ų
Envelope diameter envelope_diameter42.6
Shell Rg shell_rg18.04
Envelope Rg envelope_rg12.73
Shape Rg shape_rg12.52
Total Rg total_rg13.85
Total atoms total_atoms784
Residues n_residues101
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_real13.93
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real2.5480e+06
I(0) uncertainty (real space) i0_real_error2.6850e+04
Rg (reciprocal space) rg_reciprocal13.94
I(0) (reciprocal space) i0_reciprocal2548000.0000
Solution quality estimate total_estimate0.8960
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.049
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha363200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ayda_
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_id1aydA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain

8. Citations (4)

9. Files and Curves (10)