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7aal

Crystal structure of the F-BAR domain of PSTIPIP1, G258A mutant

Method: X-RAY DIFFRACTION Dmax: 212.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Proline-serine-threonine phosphatase-interacting protein 1

Homo sapiens

UniProt O43586

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–289 Chain B； UniProt 1–289 Mutation：G258A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；100 mM Bis-Tris-propane (pH 6.5), 15% (w/v) PEG 3350, 0.25 M sodium citrate Resolution 1.97 Å R-free 0.219

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 7AAL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2DIL Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1 Deposited 2006-03-30 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 361–416（56 aa） Fragment：SH3 domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure ambient
NMR sample composition 1.07mM SH3 domian U-15N,13C; 20mM d-Tris HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O' | 90% H2O/10% D2O
Resolution not provided
7AAM Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP Deposited 2020-09-04 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–289（289 aa）
Chain B 1–289（289 aa）
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100 mM Bis-Tris-propane (pH=6.0), 20% (w/v) PEG 3350, 200 mM sodium citrate. LYP-CTH peptide was soaked into preformed crystals of the F-BAR domain of PSTPIP1.
Resolution 2.15 Å R-free 0.241
7AAN Crystal structure of the F-BAR domain of PSTIPIP1 Deposited 2020-09-04 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–289（289 aa）
Chain B 1–289（289 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100 mM Bis-Tris-propane (pH=6.0), 17% (w/v) PEG 3350, 150 mM sodium citrate
Resolution 2.14 Å R-free 0.240

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPIP1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–292； UniProt 1–289 Author chain B； PDBConstruct 4–292； UniProt 1–289

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 7aal

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7aal
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7aal
Deposition date deposition_date2020-09-04
Structure title titleCrystal structure of the F-BAR domain of PSTIPIP1, G258A mutant
Keywords keywordspyogenic arthritis, pyoderma gangrenosum and acne (PAPA), Inflammatory response, membrane binding, SIGNALING PROTEIN; SIGNALING PROTEIN
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_guinier51.19 Å
Radius of gyration Rg (electron density) rg_electron52.74 Å
Forward intensity I(0) i074765800.00
Molecular weight molecular_weight66423.0 kDa
Excluded volume excluded_volume81794 ų
Envelope volume envelope_volume115870 ų
Hydration-shell volume shell_volume25464 ų
Envelope diameter envelope_diameter219.9 Å
Shell Rg shell_rg36.85 Å
Envelope Rg envelope_rg56.10 Å
Shape Rg shape_rg52.83 Å
Total Rg total_rg51.68 Å
Total atoms total_atoms4659
Residues n_residues570
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 dmax212.7 Å
Rg (real space) rg_real52.61 Å
Rg uncertainty (real space) rg_real_error4.36 Å
I(0) (real space) i0_real7.4770e+07
I(0) uncertainty (real space) i0_real_error1.6830e+06
Rg (reciprocal space) rg_reciprocal50.07 Å
I(0) (reciprocal space) i0_reciprocal74510000.0000
Solution quality estimate total_estimate0.6056
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.4 Å
Skewness Skewness skewness0.849
Kurtosis Kurtosis kurtosis0.154
Angular range angular_range— – 0.1550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1823000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.013; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.002; Smooth: 0.832
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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) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7aalA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily60 — Arfaptin homology (AH) domain/BAR domain
Domain ID domain_id7aalB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily60 — Arfaptin homology (AH) domain/BAR domain
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8. Citations (1)

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9. Files and Curves (10)