3aaa

Crystal Structure of Actin capping protein in complex with V-1

Method: X-RAY DIFFRACTION Dmax: 94.8 Å Quality: EXCELLENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–286 Not recorded F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.35;293 K;10% PEG 4000, 20% ISOPROPANOL, 20MM EDTA, 0.1M TRIS-HCL, pH 8.35, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.237

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–277 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) IPA ISOPROPYL ALCOHOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.35;293 K;10% PEG 4000, 20% ISOPROPANOL, 20MM EDTA, 0.1M TRIS-HCL, pH 8.35, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.237

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 1–277; UniProt 1–277

Myotrophin

Homo sapiens

UniProt P58546

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–118 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.35;293 K;10% PEG 4000, 20% ISOPROPANOL, 20MM EDTA, 0.1M TRIS-HCL, pH 8.35, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.20 Å R-free 0.237

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTPN_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–123; UniProt 1–118

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 3aaa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3aaa
Deposition date deposition_date2009-11-12
Structure title titleCrystal Structure of Actin capping protein in complex with V-1
Keywords keywordsACTIN CAPPING PROTEIN, BARBED END CAPPING, INHIBITION, PROTEIN BINDING, ACTIN CAPPING, ACTIN-BINDING, CYTOSKELETON, ANK REPEAT; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.67
Radius of gyration Rg (electron density) rg_electron28.89
Forward intensity I(0) i085278900.00
Molecular weight molecular_weight71593.0 kDa
Excluded volume excluded_volume89212 ų
Envelope volume envelope_volume112850 ų
Hydration-shell volume shell_volume32853 ų
Envelope diameter envelope_diameter98.0
Shell Rg shell_rg35.85
Envelope Rg envelope_rg29.04
Shape Rg shape_rg28.88
Total Rg total_rg29.59
Total atoms total_atoms5042
Residues n_residues634
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 dmax94.8
Rg (real space) rg_real29.66
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real8.5280e+07
I(0) uncertainty (real space) i0_real_error1.2520e+06
Rg (reciprocal space) rg_reciprocal29.67
I(0) (reciprocal space) i0_reciprocal85280000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25840000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3aaaa_
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
Domain ID domain_idd3aaab_
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.43.1.2 — Capz beta-1 subunit
Domain ID domain_idd3aaac_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamilyd.211.1 — Ankyrin repeat
Family Family familyd.211.1.1 — Ankyrin repeat

CATH v4.4 (5 domains)

Domain ID domain_id3aaaA01
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_id3aaaA02
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_id3aaaB01
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_id3aaaB02
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_id3aaaC00
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)