7w7z

Crystal Structure of human Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase

Method: X-RAY DIFFRACTION Dmax: 78.6 Å Quality: GOOD

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

Isoform 5 of Focal adhesion kinase 1

Homo sapiens

UniProt Q05397

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 902–1065 Fragment:Focal adhesion targeting domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;1.0 M Lithium sulfate 0.1 M MES pH 6.5 Resolution 2.15 Å R-free 0.239

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.

38 other PDB entries and 81 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAK1_HUMAN
Isoform Q05397-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–164; UniProt 902–1065

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 7w7z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w7z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7w7z
Deposition date deposition_date2021-12-07
Structure title titleCrystal Structure of human Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase
Keywords keywordsFocal adhesion kinase, Protein tyrosine kinase 2, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.20
Radius of gyration Rg (electron density) rg_electron22.43
Forward intensity I(0) i04724040.00
Molecular weight molecular_weight16087.0 kDa
Excluded volume excluded_volume20346 ų
Envelope volume envelope_volume30317 ų
Hydration-shell volume shell_volume12675 ų
Envelope diameter envelope_diameter80.5
Shell Rg shell_rg26.67
Envelope Rg envelope_rg22.46
Shape Rg shape_rg22.44
Total Rg total_rg23.10
Total atoms total_atoms1125
Residues n_residues145
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 dmax78.6
Rg (real space) rg_real23.33
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real4.7240e+06
I(0) uncertainty (real space) i0_real_error7.2590e+04
Rg (reciprocal space) rg_reciprocal23.31
I(0) (reciprocal space) i0_reciprocal4724000.0000
Solution quality estimate total_estimate0.8358
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.788
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha314400.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.590; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)