9ifk

Crystal structure of Kalirin/Rac1 in complex with DK-2

Method: X-RAY DIFFRACTION Dmax: 71.8 Å Quality: GOOD

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

Ras-related C3 botulinum toxin substrate 1

Homo sapiens

UniProt P63000

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–177 Not recorded Kalirin × 1 (P97924) A1I32 2-chloranyl-~{N}-(2-oxidanylidene-1~{H}-quinolin-4-yl)ethanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M citrate pH 4.7, 0.8 M LiCl and 25% PEG 6K. Resolution 1.34 Å R-free 0.235

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.

74 other PDB entries and 102 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–177; UniProt 1–177

Kalirin

Rattus norvegicus

UniProt P97924

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1253–1432 Fragment:UNP residues 1253-1432 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) A1I32 2-chloranyl-~{N}-(2-oxidanylidene-1~{H}-quinolin-4-yl)ethanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M citrate pH 4.7, 0.8 M LiCl and 25% PEG 6K. Resolution 1.34 Å R-free 0.235

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KALRN_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–180; UniProt 1253–1432

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 9ifk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ifk
Deposition date deposition_date2025-02-18
最后修订 last_revision2026-03-04
Structure title titleCrystal structure of Kalirin/Rac1 in complex with DK-2
Keywords keywordsGTPase, guanine nucleotide exchange factor, complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.14
Radius of gyration Rg (electron density) rg_electron20.39
Forward intensity I(0) i043888600.00
Molecular weight molecular_weight35078.0 kDa
Excluded volume excluded_volume34288 ų
Envelope volume envelope_volume54807 ų
Hydration-shell volume shell_volume22298 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg27.07
Envelope Rg envelope_rg20.62
Shape Rg shape_rg20.39
Total Rg total_rg21.04
Total atoms total_atoms2658
Residues n_residues344
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 dmax71.8
Rg (real space) rg_real21.04
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.3890e+07
I(0) uncertainty (real space) i0_real_error5.4970e+05
Rg (reciprocal space) rg_reciprocal21.06
I(0) (reciprocal space) i0_reciprocal43890000.0000
Solution quality estimate total_estimate0.8772
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9641000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)