5d68

Crystal structure of KRIT1 ARD-FERM

Method: X-RAY DIFFRACTION Dmax: 173.1 Å Quality: GOOD

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

Krev interaction trapped protein 1

Homo sapiens

UniProt O00522

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 52–529 Fragment:ARD-FERM domain (UNP residues 52-529) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;298 K;0.05 M HEPES, pH 7.3, 8% ethylene glycol, 8% PEG8000 Resolution 2.91 Å R-free 0.246
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 52–529 Fragment:ARD-FERM domain (UNP residues 52-529) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;298 K;0.05 M HEPES, pH 7.3, 8% ethylene glycol, 8% PEG8000 Resolution 2.91 Å R-free 0.246
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 52–529 Fragment:ARD-FERM domain (UNP residues 52-529) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;298 K;0.05 M HEPES, pH 7.3, 8% ethylene glycol, 8% PEG8000 Resolution 2.91 Å R-free 0.246

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.

14 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KRIT1_HUMAN
Isoform O00522-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–486; UniProt 52–529 Author chain B; PDBConstruct 9–486; UniProt 52–529 Author chain C; PDBConstruct 9–486; UniProt 52–529

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 5d68

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d68
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5d68
Deposition date deposition_date2015-08-11
Structure title titleCrystal structure of KRIT1 ARD-FERM
Keywords keywordsAnkyrin Repeat Domain, FERM domain, Cerebral Cavernous Malformations, 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_guinier47.27
Radius of gyration Rg (electron density) rg_electron47.09
Forward intensity I(0) i0324290000.00
Molecular weight molecular_weight150330.0 kDa
Excluded volume excluded_volume189340 ų
Envelope volume envelope_volume281040 ų
Hydration-shell volume shell_volume52728 ų
Envelope diameter envelope_diameter168.5
Shell Rg shell_rg47.73
Envelope Rg envelope_rg46.12
Shape Rg shape_rg47.10
Total Rg total_rg47.06
Total atoms total_atoms10586
Residues n_residues1301
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 dmax173.1
Rg (real space) rg_real47.65
Rg uncertainty (real space) rg_real_error2.29
I(0) (real space) i0_real3.2430e+08
I(0) uncertainty (real space) i0_real_error7.0050e+06
Rg (reciprocal space) rg_reciprocal47.27
I(0) (reciprocal space) i0_reciprocal324100000.0000
Solution quality estimate total_estimate0.7844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.464
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15550000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.773; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)