4jif

Co-crystal structure of ICAP1 PTB domain in complex with a KRIT1 peptide

Method: X-RAY DIFFRACTION Dmax: 50.2 Å Quality: GOOD

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

Integrin beta-1-binding protein 1

Homo sapiens

UniProt O14713

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 49–200 Not recorded Krev interaction trapped protein 1 × 1 (O00522) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;18-20%PEG3350, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 49–200 Not recorded Krev interaction trapped protein 1 × 2 (O00522) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;18-20%PEG3350, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.226

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.

2 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–154; UniProt 49–200

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 170–198 Not recorded Integrin beta-1-binding protein 1 × 1 (O14713) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;18-20%PEG3350, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 170–198 Not recorded Integrin beta-1-binding protein 1 × 2 (O14713) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;18-20%PEG3350, 0.2M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.226

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KRIT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–34; UniProt 170–198

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 4jif

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4jif
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4jif
Deposition date deposition_date2013-03-05
Structure title titleCo-crystal structure of ICAP1 PTB domain in complex with a KRIT1 peptide
Keywords keywordsPTB fold, Integrin signaling, Integrin binding, 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_guinier15.93
Radius of gyration Rg (electron density) rg_electron14.54
Forward intensity I(0) i05068780.00
Molecular weight molecular_weight16691.0 kDa
Excluded volume excluded_volume21179 ų
Envelope volume envelope_volume23776 ų
Hydration-shell volume shell_volume13680 ų
Envelope diameter envelope_diameter49.6
Shell Rg shell_rg20.62
Envelope Rg envelope_rg14.89
Shape Rg shape_rg14.56
Total Rg total_rg15.73
Total atoms total_atoms1175
Residues n_residues149
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 dmax50.2
Rg (real space) rg_real15.80
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real5.0690e+06
I(0) uncertainty (real space) i0_real_error5.3980e+04
Rg (reciprocal space) rg_reciprocal15.82
I(0) (reciprocal space) i0_reciprocal5069000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1152000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4jifA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

8. Citations (1)

9. Files and Curves (10)