2crh

Solution structure of the SH2 domain of human proto-oncogene protein VAV1

Method: SOLUTION NMR Dmax: 50.2 Å Quality: REASONABLE

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

Vav proto-oncogene

Homo sapiens

UniProt P15498

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 629–775 Fragment:SH2 (residues 1-138) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120 mM;Pressure ambient NMR sample composition:1.15mM 13C,15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3 | 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.

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

View Construct and Data Evidence
UniProt name VAV_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–132; UniProt 629–775

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 2crh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2crh
Deposition date deposition_date2005-05-20
Structure title titleSolution structure of the SH2 domain of human proto-oncogene protein VAV1
Keywords keywords;ONCOPROTEIN, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.62
Radius of gyration Rg (electron density) rg_electron17.64
Forward intensity I(0) i01360730000.00
Molecular weight molecular_weight309190.0 kDa
Excluded volume excluded_volume386130 ų
Envelope volume envelope_volume102520 ų
Hydration-shell volume shell_volume30916 ų
Envelope diameter envelope_diameter113.5
Shell Rg shell_rg34.47
Envelope Rg envelope_rg29.91
Shape Rg shape_rg17.61
Total Rg total_rg18.24
Total atoms total_atoms43280
Residues n_residues2760
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 dmax50.2
Rg (real space) rg_real17.20
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real1.2900e+09
I(0) uncertainty (real space) i0_real_error1.2780e+07
Rg (reciprocal space) rg_reciprocal18.89
I(0) (reciprocal space) i0_reciprocal1361000000.0000
Solution quality estimate total_estimate0.6746
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha3.1480
Highest regularization parameter α highest_alpha741400.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.008; Oscil: 0.938; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; 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_idd2crha1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.0 — automated matches
Domain ID domain_idd2crha2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2crha3
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_id2crhA01
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)