9irl

Crystal structure analysis of LW-Srci-2o in complex with c-Src.

Method: X-RAY DIFFRACTION Dmax: 79.5 Å Quality: EXCELLENT

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

Proto-oncogene tyrosine-protein kinase Src

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 86–536 Non-standard monomer:Yes (specific site not provided by mmCIF) A1L20 (2~{R})-2-[3,5-bis(fluoranyl)phenyl]-2-[2-chloranylethanoyl(cyclopropyl)amino]-~{N}-cyclopentyl-ethanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;PEG 3350, Hepes 7.4 Resolution 2.03 Å R-free 0.243

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 101 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 1–451; UniProt 86–536

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 9irl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9irl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9irl
Deposition date deposition_date2024-07-16
最后修订 last_revision2025-07-16
Structure title titleCrystal structure analysis of LW-Srci-2o in complex with c-Src.
Keywords keywordscovalent inhibitor, c-Src kinase, allosteric pocket, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.25
Radius of gyration Rg (electron density) rg_electron24.44
Forward intensity I(0) i084451500.00
Molecular weight molecular_weight48125.0 kDa
Excluded volume excluded_volume46536 ų
Envelope volume envelope_volume79528 ų
Hydration-shell volume shell_volume27351 ų
Envelope diameter envelope_diameter81.2
Shell Rg shell_rg31.53
Envelope Rg envelope_rg24.34
Shape Rg shape_rg24.43
Total Rg total_rg25.06
Total atoms total_atoms3642
Residues n_residues450
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 dmax79.5
Rg (real space) rg_real25.20
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real8.4450e+07
I(0) uncertainty (real space) i0_real_error9.8580e+05
Rg (reciprocal space) rg_reciprocal25.21
I(0) (reciprocal space) i0_reciprocal84450000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17610000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)