3t9k

Crystal Structure of ACAP1 C-portion mutant S554D fused with integrin beta1 peptide

Method: X-RAY DIFFRACTION Dmax: 96.7 Å Quality: GOOD

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

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1,Peptide from Integrin beta-1

Homo sapiens

UniProt P05556

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 758–769 Mutation:S554D ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;289 K;0.2M ammonium sulfate, 14% PEG 3350, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.30 Å R-free 0.225
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 758–769 Mutation:S554D ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;289 K;0.2M ammonium sulfate, 14% PEG 3350, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.30 Å R-free 0.225

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.

21 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 379–390; UniProt 758–769 Author chain B; PDBConstruct 379–390; UniProt 758–769

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1,Peptide from Integrin beta-1

Homo sapiens

UniProt Q15027

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 378–740 Mutation:S554D ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;289 K;0.2M ammonium sulfate, 14% PEG 3350, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.30 Å R-free 0.225
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 378–740 Mutation:S554D ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;289 K;0.2M ammonium sulfate, 14% PEG 3350, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.30 Å R-free 0.225

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACAP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–368; UniProt 378–740 Author chain B; PDBConstruct 6–368; UniProt 378–740

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 3t9k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3t9k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3t9k
Deposition date deposition_date2011-08-03
Structure title titleCrystal Structure of ACAP1 C-portion mutant S554D fused with integrin beta1 peptide
Keywords keywordsArfGAP domain, ANK repeat, zinc-binding module, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.26
Radius of gyration Rg (electron density) rg_electron28.59
Forward intensity I(0) i061747500.00
Molecular weight molecular_weight58991.0 kDa
Excluded volume excluded_volume72870 ų
Envelope volume envelope_volume93667 ų
Hydration-shell volume shell_volume28608 ų
Envelope diameter envelope_diameter97.1
Shell Rg shell_rg34.39
Envelope Rg envelope_rg28.34
Shape Rg shape_rg28.62
Total Rg total_rg29.09
Total atoms total_atoms4126
Residues n_residues554
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 dmax96.7
Rg (real space) rg_real29.34
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real6.1750e+07
I(0) uncertainty (real space) i0_real_error9.7420e+05
Rg (reciprocal space) rg_reciprocal29.31
I(0) (reciprocal space) i0_reciprocal61750000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9793000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3t9kA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily150 — Arf GTPase activating protein
Domain ID domain_id3t9kA02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id3t9kB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology220 — Annexin V; domain 1
Homologous superfamily homologous superfamily150 — Arf GTPase activating protein
Domain ID domain_id3t9kB02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (1)

9. Files and Curves (10)