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1csk

THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP

Method: X-RAY DIFFRACTION Dmax: 70.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

C-SRC SH3 DOMAIN

Homo sapiens

UniProt P41240

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 1–71 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å R-free 0.278
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 1–71 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å R-free 0.278
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain C； UniProt 1–71 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å R-free 0.278
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain D； UniProt 1–71 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 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.

Other PDB Difference from Current Entry 1CSK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BYG KINASE DOMAIN OF HUMAN C-TERMINAL SRC KINASE (CSK) IN COMPLEX WITH INHIBITOR STAUROSPORINE Deposited 1998-10-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 173–450（278 aa） Fragment：KINASE DOMAIN
Not recorded STU STAUROSPORINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；VAPOUR DIFFUSION, PROTEIN SOLUTION (10 MG/ML) CONTAINING 1MM STAUROSPORINE WAS MIXED IN 1:1 RATIO WITH THE RESERVOIR SOLUTION. THE RESERVOIR SOLUTION CONTAINED 0.2M MGCL2, 0.1M TRISHCL PH 9.0, 24% PEG 4000.
Resolution 2.40 Å R-free 0.287
3D7T Structural basis for the recognition of c-Src by its inactivator Csk Deposited 2008-05-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 188–450（263 aa） Fragment：Csk kinase domain
Mutation：K361A/K362A STU STAUROSPORINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；VAPOR DIFFUSION, SITTING DROP
Resolution 2.90 Å R-free 0.278
3D7T Structural basis for the recognition of c-Src by its inactivator Csk Deposited 2008-05-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 188–450（263 aa） Fragment：Csk kinase domain
Mutation：K361A/K362A STU STAUROSPORINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；VAPOR DIFFUSION, SITTING DROP
Resolution 2.90 Å R-free 0.278
3D7U Structural basis for the recognition of c-Src by its inactivator Csk Deposited 2008-05-21 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 188–450（263 aa） Fragment：Csk kinase domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 4.11 Å R-free 0.302
3D7U Structural basis for the recognition of c-Src by its inactivator Csk Deposited 2008-05-21 Different construct Different oligomeric state Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 188–450（263 aa） Fragment：Csk kinase domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 4.11 Å R-free 0.302
3EAC Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), Oxidized form. Deposited 2008-08-25 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 73–178（106 aa） Fragment：SH2 Domain (UNP residues 73 to 178)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.3；298 K；22% PEG 4000, 100 mM Bis-Tris, pH 7.3., EVAPORATION, temperature 298K
Resolution 1.37 Å R-free 0.217
3EAZ Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), C122S mutant. Deposited 2008-08-26 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 73–178（106 aa） Fragment：Csk, SH2 domain (UNP residues 73 to 178)
Mutation：C122S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；298 K；22% PEG 4000, 100 mM Bis-Tris, pH 7.3., VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.31 Å R-free 0.226

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSK_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–71； UniProt 1–71 Author chain B； PDBConstruct 1–71； UniProt 1–71 Author chain C； PDBConstruct 1–71； UniProt 1–71 Author chain D； PDBConstruct 1–71； UniProt 1–71

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 1csk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1csk
Deposition date deposition_date1994-03-22
Structure title titleTHE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP
Keywords keywordsPHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.22 Å
Radius of gyration Rg (electron density) rg_electron20.53 Å
Forward intensity I(0) i011444900.00
Molecular weight molecular_weight25870.0 kDa
Excluded volume excluded_volume32645 ų
Envelope volume envelope_volume39982 ų
Hydration-shell volume shell_volume16847 ų
Envelope diameter envelope_diameter73.9 Å
Shell Rg shell_rg26.15 Å
Envelope Rg envelope_rg20.46 Å
Shape Rg shape_rg20.45 Å
Total Rg total_rg21.61 Å
Total atoms total_atoms1824
Residues n_residues232
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax70.1 Å
Rg (real space) rg_real21.22 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real1.1440e+07
I(0) uncertainty (real space) i0_real_error1.4900e+05
Rg (reciprocal space) rg_reciprocal21.22 Å
I(0) (reciprocal space) i0_reciprocal11440000.0000
Solution quality estimate total_estimate0.8054
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.6 Å
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6882000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.911; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cska_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain
Domain ID domain_idd1cskb_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain
Domain ID domain_idd1cskc_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain
Domain ID domain_idd1cskd_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (4 domains)

Domain ID domain_id1cskA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1cskB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1cskC00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1cskD00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
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8. Citations (1)

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9. Files and Curves (10)