1xba

Crystal structure of apo syk tyrosine kinase domain

Method: X-RAY DIFFRACTION Dmax: 61.3 Å Quality: GOOD

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

Tyrosine-protein kinase SYK

Homo sapiens

UniProt P43405

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 353–635 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;15% peg 3350, 100mM Tris HCl (pH 8.5) Resolution 2.00 Å R-free 0.278

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.

92 other PDB entries and 134 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KSYK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–283; UniProt 353–635

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 1xba

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xba
Deposition date deposition_date2004-08-30
Structure title titleCrystal structure of apo syk tyrosine kinase domain
Keywords keywordsspleen typrosine kinase, active conformation, structural genomics, Structural GenomiX, Transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.45
Radius of gyration Rg (electron density) rg_electron18.47
Forward intensity I(0) i014473500.00
Molecular weight molecular_weight29415.0 kDa
Excluded volume excluded_volume37065 ų
Envelope volume envelope_volume42206 ų
Hydration-shell volume shell_volume19095 ų
Envelope diameter envelope_diameter62.2
Shell Rg shell_rg24.84
Envelope Rg envelope_rg18.75
Shape Rg shape_rg18.46
Total Rg total_rg19.42
Total atoms total_atoms2068
Residues n_residues266
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 dmax61.3
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.4470e+07
I(0) uncertainty (real space) i0_real_error1.6720e+05
Rg (reciprocal space) rg_reciprocal19.37
I(0) (reciprocal space) i0_reciprocal14470000.0000
Solution quality estimate total_estimate0.8201
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5186000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1xbaa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit
Domain ID domain_idd1xbaa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1xbaA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id1xbaA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)