9bli

Crystal structure of Actin capping protein in complex with a fragment of Legionella pneumophila RavB

Method: X-RAY DIFFRACTION Dmax: 94.0 Å Quality: REASONABLE

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

F-actin-capping protein subunit alpha-1

Gallus gallus

UniProt P13127

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–286 Not recorded F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) Integrase × 1 (Q5ZZI0) FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;10 mM Tris pH 8.0, 0.2 M ammonium formate, 0.15 M NaCl, 21% w/v PEG 3350, 30% ethylene glycol Resolution 2.00 Å R-free 0.208

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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAZA1_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–286; UniProt 1–286

F-actin-capping protein subunit beta isoforms 1 and 2

Gallus gallus

UniProt P14315

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–244 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) Integrase × 1 (Q5ZZI0) FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;10 mM Tris pH 8.0, 0.2 M ammonium formate, 0.15 M NaCl, 21% w/v PEG 3350, 30% ethylene glycol Resolution 2.00 Å R-free 0.208

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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPZB_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–248; UniProt 1–244

Integrase

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

UniProt Q5ZZI0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 108–149 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;10 mM Tris pH 8.0, 0.2 M ammonium formate, 0.15 M NaCl, 21% w/v PEG 3350, 30% ethylene glycol Resolution 2.00 Å R-free 0.208

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q5ZZI0_LEGPH
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–42; UniProt 108–149

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 9bli

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bli
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bli
Deposition date deposition_date2024-04-30
Structure title titleCrystal structure of Actin capping protein in complex with a fragment of Legionella pneumophila RavB
Keywords keywords;ACTIN CAPPING PROTEIN, BARBED END REGULATION, CONFORMATIONAL CHANGE, CELL MOTILITY, ACTIN CAPPING, ACTIN-BINDING, CYTOSKELETON, PROTEIN BINDING, SECRETED BACTERIAL EFFECTOR PROTEIN ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.97
Radius of gyration Rg (electron density) rg_electron27.16
Forward intensity I(0) i067057600.00
Molecular weight molecular_weight62453.0 kDa
Excluded volume excluded_volume77535 ų
Envelope volume envelope_volume96013 ų
Hydration-shell volume shell_volume29970 ų
Envelope diameter envelope_diameter95.5
Shell Rg shell_rg34.02
Envelope Rg envelope_rg27.46
Shape Rg shape_rg27.15
Total Rg total_rg27.89
Total atoms total_atoms8694
Residues n_residues547
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 dmax94.0
Rg (real space) rg_real28.07
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real6.7060e+07
I(0) uncertainty (real space) i0_real_error9.1930e+05
Rg (reciprocal space) rg_reciprocal28.04
I(0) (reciprocal space) i0_reciprocal67060000.0000
Solution quality estimate total_estimate0.6647
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha23810000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 0.075; Positv: 1.000; Valcen: 0.944; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)