3aa6

Crystal structure of Actin capping protein in complex with the Cp-binding motif derived from CD2AP

Method: X-RAY DIFFRACTION Dmax: 93.8 Å Quality: GOOD

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) 23mer peptide from CD2-associated protein × 1 (Q9Y5K6) BA BARIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;10% PEG 400, 20MM BACL2, 100MM MES-NAOH, PH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 1.90 Å R-free 0.238

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 Mutation:residues 244-277 deletion mutation F-actin-capping protein subunit alpha-1 × 1 (P13127) 23mer peptide from CD2-associated protein × 1 (Q9Y5K6) BA BARIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;10% PEG 400, 20MM BACL2, 100MM MES-NAOH, PH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 1.90 Å R-free 0.238

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 1–244; UniProt 1–244

23mer peptide from CD2-associated protein

OrganismNot specified

UniProt Q9Y5K6

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 485–507 Fragment:recidues 485-507 F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) BA BARIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;10% PEG 400, 20MM BACL2, 100MM MES-NAOH, PH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 1.90 Å R-free 0.238

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.

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

View Construct and Data Evidence
UniProt name CD2AP_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–23; UniProt 485–507

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 3aa6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3aa6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3aa6
Deposition date deposition_date2009-11-11
Structure title titleCrystal structure of Actin capping protein in complex with the Cp-binding motif derived from CD2AP
Keywords keywords;ACTIN CAPPING PROTEIN, BARBED END REGULATION, CARMIL FAMILY PROTEIN, CONFORMATIONAL CHANGE, CELL MOTILITY, CD2AP, Actin capping, Actin-binding, Cytoskeleton, Cell cycle, Cell division, Cell projection, Mitosis, SH3 domain, SH3-binding, 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_guinier27.85
Radius of gyration Rg (electron density) rg_electron27.09
Forward intensity I(0) i063635000.00
Molecular weight molecular_weight61036.0 kDa
Excluded volume excluded_volume75774 ų
Envelope volume envelope_volume92252 ų
Hydration-shell volume shell_volume29130 ų
Envelope diameter envelope_diameter97.1
Shell Rg shell_rg33.74
Envelope Rg envelope_rg27.37
Shape Rg shape_rg27.09
Total Rg total_rg27.78
Total atoms total_atoms4291
Residues n_residues535
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 dmax93.8
Rg (real space) rg_real27.98
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real6.3630e+07
I(0) uncertainty (real space) i0_real_error1.0100e+06
Rg (reciprocal space) rg_reciprocal27.94
I(0) (reciprocal space) i0_reciprocal63630000.0000
Solution quality estimate total_estimate0.8746
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha23270000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3aa6a_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.43 — Subunits of heterodimeric actin filament capping protein Capz
Superfamily Superfamily superfamilye.43.1 — Subunits of heterodimeric actin filament capping protein Capz
Family Family familye.43.1.1 — Capz alpha-1 subunit

CATH v4.4 (4 domains)

Domain ID domain_id3aa6A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1140 — Ribosomal protein S3 C-terminal domain
Homologous superfamily homologous superfamily60 — F-actin capping protein, alpha subunit
Domain ID domain_id3aa6A02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily210 — F-actin capping protein, beta subunit
Domain ID domain_id3aa6B01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily570 — F-actin capping protein, alpha/beta subunit, N-terminal domain
Domain ID domain_id3aa6B02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily210 — F-actin capping protein, beta subunit

8. Citations (1)

9. Files and Curves (10)