2w10

Mona SH3C in complex

Method: X-RAY DIFFRACTION Dmax: 61.0 Å Quality: GOOD

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

GRB2-RELATED ADAPTOR PROTEIN 2

MUS MUSCULUS

UniProt O89100

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 265–322 Fragment:SH3 2, RESIDUES 265-322 TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23 × 1 (Q6PB44) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5 Resolution 1.90 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 265–322 Fragment:SH3 2, RESIDUES 265-322 TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23 × 1 (Q6PB44) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5 Resolution 1.90 Å R-free 0.231

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.

7 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRAP2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–62; UniProt 265–322 Author chain B; PDBConstruct 5–62; UniProt 265–322

TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23

OrganismNot specified

UniProt Q6PB44

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 719–730 Fragment:SH3 BINDING REGION, RESIDUES 719-730 GRB2-RELATED ADAPTOR PROTEIN 2 × 1 (O89100) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5 Resolution 1.90 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 719–730 Fragment:SH3 BINDING REGION, RESIDUES 719-730 GRB2-RELATED ADAPTOR PROTEIN 2 × 1 (O89100) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M PHOSPHATE CITRATE, 2 M AMMONIUM SULPHATE, pH 7.5 Resolution 1.90 Å R-free 0.231

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PTN23_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–12; UniProt 719–730 Author chain D; PDBConstruct 1–12; UniProt 719–730

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 2w10

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2w10
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2w10
Deposition date deposition_date2008-10-13
Structure title titleMona SH3C in complex
Keywords keywords;ALTERNATIVE SPLICING, TPR REPEAT, SH2 DOMAIN, SH3 DOMAIN, COILED COIL, PROTEIN PHOSPHATASE, CYTOPLASMIC VESICLE, PHOSPHOPROTEIN, SIGNAL TRANDUCTION, SH3 DOMAIN-COMPLEX, SH3, GADS, MONA, DIMER, HD-PTP, HYDROLASE, CYTOPLASM ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.79
Radius of gyration Rg (electron density) rg_electron17.37
Forward intensity I(0) i05117310.00
Molecular weight molecular_weight16370.0 kDa
Excluded volume excluded_volume20479 ų
Envelope volume envelope_volume24198 ų
Hydration-shell volume shell_volume12669 ų
Envelope diameter envelope_diameter60.3
Shell Rg shell_rg21.95
Envelope Rg envelope_rg17.63
Shape Rg shape_rg17.40
Total Rg total_rg18.13
Total atoms total_atoms1156
Residues n_residues144
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 dmax61.0
Rg (real space) rg_real17.90
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.1170e+06
I(0) uncertainty (real space) i0_real_error6.1150e+04
Rg (reciprocal space) rg_reciprocal17.89
I(0) (reciprocal space) i0_reciprocal5117000.0000
Solution quality estimate total_estimate0.8472
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.211
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2439000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2w10a_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain
Domain ID domain_idd2w10b_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (2 domains)

Domain ID domain_id2w10A00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id2w10B00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains

8. Citations (1)

9. Files and Curves (10)