8ze8

Arf-GTPase activating protein Asap1 SH3 domain in complex with 440 Kd Ankyrin-B fragment

Method: X-RAY DIFFRACTION Dmax: 73.6 Å Quality: EXCELLENT

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

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1

Mus musculus

UniProt Q9QWY8

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 1083–1147 Not recorded Ankyrin-2 × 1 (Q01484) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1083–1147 Not recorded Ankyrin-2 × 1 (Q01484) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1083–1147 Not recorded Ankyrin-2 × 1 (Q01484) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1083–1147 Not recorded Ankyrin-2 × 1 (Q01484) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 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.

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

View Construct and Data Evidence
UniProt name ASAP1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–69; UniProt 1083–1147 Author chain B; PDBConstruct 5–69; UniProt 1083–1147 Author chain D; PDBConstruct 5–69; UniProt 1083–1147 Author chain G; PDBConstruct 5–69; UniProt 1083–1147

Ankyrin-2

OrganismNot specified

UniProt Q01484

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 E; UniProt 1699–1710 Not recorded Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 × 1 (Q9QWY8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1699–1710 Not recorded Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 × 1 (Q9QWY8) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1699–1710 Not recorded Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 × 1 (Q9QWY8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 Å R-free 0.226
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1699–1710 Not recorded Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 × 1 (Q9QWY8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M MES monohydrate, pH=6.0, 20 % w/v Polyethylene glycol 6,000 Resolution 2.07 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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANK2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–12; UniProt 1699–1710 Author chain E; PDBConstruct 1–12; UniProt 1699–1710 Author chain F; PDBConstruct 1–12; UniProt 1699–1710 Author chain H; PDBConstruct 1–12; UniProt 1699–1710

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 8ze8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ze8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ze8
Deposition date deposition_date2024-05-04
Structure title titleArf-GTPase activating protein Asap1 SH3 domain in complex with 440 Kd Ankyrin-B fragment
Keywords keywordscomplex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.73
Radius of gyration Rg (electron density) rg_electron22.68
Forward intensity I(0) i017330200.00
Molecular weight molecular_weight31623.0 kDa
Excluded volume excluded_volume39640 ų
Envelope volume envelope_volume50736 ų
Hydration-shell volume shell_volume19255 ų
Envelope diameter envelope_diameter75.9
Shell Rg shell_rg28.67
Envelope Rg envelope_rg22.36
Shape Rg shape_rg22.67
Total Rg total_rg23.52
Total atoms total_atoms4400
Residues n_residues274
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 dmax73.6
Rg (real space) rg_real23.61
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.7330e+07
I(0) uncertainty (real space) i0_real_error2.0640e+05
Rg (reciprocal space) rg_reciprocal23.64
I(0) (reciprocal space) i0_reciprocal17330000.0000
Solution quality estimate total_estimate0.9009
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.6
Skewness Skewness skewness0.051
Kurtosis Kurtosis kurtosis-0.657
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6044000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)