2dlz

Solution structure of the SH2 domain of human protein vav-2

Method: SOLUTION NMR Dmax: 55.8 Å Quality: REASONABLE

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

Protein vav-2

Homo sapiens

UniProt P52735

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 663–767 Fragment:sh2 domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.16mM 13C,15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 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.

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAV2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–112; UniProt 663–767

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 2dlz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2dlz
Deposition date deposition_date2006-04-20
Structure title titleSolution structure of the SH2 domain of human protein vav-2
Keywords keywords;Rho family Guanine nucleotide exchange factor, 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_guinier15.16
Radius of gyration Rg (electron density) rg_electron14.30
Forward intensity I(0) i01026220000.00
Molecular weight molecular_weight269860.0 kDa
Excluded volume excluded_volume336470 ų
Envelope volume envelope_volume39864 ų
Hydration-shell volume shell_volume18174 ų
Envelope diameter envelope_diameter60.3
Shell Rg shell_rg25.00
Envelope Rg envelope_rg19.44
Shape Rg shape_rg14.26
Total Rg total_rg14.64
Total atoms total_atoms37540
Residues n_residues2360
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 dmax55.8
Rg (real space) rg_real15.13
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.0260e+09
I(0) uncertainty (real space) i0_real_error1.3350e+07
Rg (reciprocal space) rg_reciprocal15.14
I(0) (reciprocal space) i0_reciprocal1026000000.0000
Solution quality estimate total_estimate0.6414
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis0.112
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha439200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.542; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.942; Smooth: 0.997

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_idd2dlza1
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_idd2dlza2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2dlza3
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_id2dlzA01
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)