1a09

C-src (SH2 domain) complexed with ace-formyl phosphotyr-glu-(n,n-dipentyl amine)

Method: X-RAY DIFFRACTION Dmax: 64.1 Å Quality: GOOD

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

C-SRC TYROSINE KINASE

Homo sapiens

UniProt P12931

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 143–248 Chain B; UniProt 143–248 Fragment:SH2 DOMAIN ACE-FORMYL PHOSPHOTYR-GLU-(N,N-DIPENTYL AMINE) × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;277 K;PROTEIN WAS CRYSTALLIZED FROM 0.1 M ACETATE, PH 4.6, 2 M NAFORMATE AT 4 C. THE CRYSTAL WAS SOAKED IN 10% PEG400, 10% GLYCEROL PRIOR TO DATA COLLECTION, temperature 277K Resolution 2.00 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 143–248 Fragment:SH2 DOMAIN ACE-FORMYL PHOSPHOTYR-GLU-(N,N-DIPENTYL AMINE) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;277 K;PROTEIN WAS CRYSTALLIZED FROM 0.1 M ACETATE, PH 4.6, 2 M NAFORMATE AT 4 C. THE CRYSTAL WAS SOAKED IN 10% PEG400, 10% GLYCEROL PRIOR TO DATA COLLECTION, temperature 277K Resolution 2.00 Å
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 143–248 Fragment:SH2 DOMAIN ACE-FORMYL PHOSPHOTYR-GLU-(N,N-DIPENTYL AMINE) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;277 K;PROTEIN WAS CRYSTALLIZED FROM 0.1 M ACETATE, PH 4.6, 2 M NAFORMATE AT 4 C. THE CRYSTAL WAS SOAKED IN 10% PEG400, 10% GLYCEROL PRIOR TO DATA COLLECTION, temperature 277K Resolution 2.00 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.

76 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–107; UniProt 143–248 Author chain B; PDBConstruct 2–107; UniProt 143–248

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 1a09

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a09
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a09
Deposition date deposition_date1997-12-10
Structure title titleC-src (SH2 domain) complexed with ace-formyl phosphotyr-glu-(n,n-dipentyl amine)
Keywords keywordsCOMPLEX (TRANSFERASE-PEPTIDE), COMPLEX (TRANSFERASE-PEPTIDE) complex; COMPLEX (TRANSFERASE/PEPTIDE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.72
Radius of gyration Rg (electron density) rg_electron18.94
Forward intensity I(0) i011288200.00
Molecular weight molecular_weight24713.0 kDa
Excluded volume excluded_volume30815 ų
Envelope volume envelope_volume36091 ų
Hydration-shell volume shell_volume16557 ų
Envelope diameter envelope_diameter63.8
Shell Rg shell_rg24.25
Envelope Rg envelope_rg19.13
Shape Rg shape_rg18.97
Total Rg total_rg19.67
Total atoms total_atoms2151
Residues n_residues210
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 dmax64.1
Rg (real space) rg_real19.74
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.1290e+07
I(0) uncertainty (real space) i0_real_error1.3880e+05
Rg (reciprocal space) rg_reciprocal19.74
I(0) (reciprocal space) i0_reciprocal11290000.0000
Solution quality estimate total_estimate0.7521
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.364
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1903000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 0.424; Positv: 1.000; Valcen: 0.975; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a09a_
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
Domain ID domain_idd1a09b_
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 (2 domains)

Domain ID domain_id1a09A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1a09B00
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)