1izn

Crystal Structure of Actin Filament Capping Protein CapZ

Method: X-RAY DIFFRACTION Dmax: 182.6 Å Quality: REASONABLE

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

CapZ alpha-1 subunit

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 CapZ beta-1 subunit × 1 (P14315) NO3 NITRATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;PEG3350, magnesium nitrate, MES-NAOH, Jeffamine M-600, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.10 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–286 Not recorded CapZ beta-1 subunit × 1 (P14315) NO3 NITRATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;PEG3350, magnesium nitrate, MES-NAOH, Jeffamine M-600, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.10 Å R-free 0.262

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 34 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 Author chain C; PDBConstruct 1–286; UniProt 1–286

CapZ beta-1 subunit

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 CapZ alpha-1 subunit × 1 (P13127) NO3 NITRATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;PEG3350, magnesium nitrate, MES-NAOH, Jeffamine M-600, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.10 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–277 Not recorded CapZ alpha-1 subunit × 1 (P13127) NO3 NITRATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;PEG3350, magnesium nitrate, MES-NAOH, Jeffamine M-600, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K Resolution 2.10 Å R-free 0.262

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 34 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 Author chain D; PDBConstruct 1–277; UniProt 1–277

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 1izn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1izn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1izn
Deposition date deposition_date2002-10-10
Structure title titleCrystal Structure of Actin Filament Capping Protein CapZ
Keywords keywordsHETERODIMER, CAPPING PROTEIN, ACTIN FILAMENT BARBED END CAPPING, 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_guinier48.52
Radius of gyration Rg (electron density) rg_electron49.95
Forward intensity I(0) i0240869000.00
Molecular weight molecular_weight124330.0 kDa
Excluded volume excluded_volume154410 ų
Envelope volume envelope_volume222360 ų
Hydration-shell volume shell_volume42743 ų
Envelope diameter envelope_diameter174.9
Shell Rg shell_rg43.52
Envelope Rg envelope_rg50.41
Shape Rg shape_rg49.96
Total Rg total_rg49.64
Total atoms total_atoms8759
Residues n_residues1088
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 dmax182.6
Rg (real space) rg_real49.78
Rg uncertainty (real space) rg_real_error2.76
I(0) (real space) i0_real2.4090e+08
I(0) uncertainty (real space) i0_real_error4.6010e+06
Rg (reciprocal space) rg_reciprocal48.53
I(0) (reciprocal space) i0_reciprocal240500000.0000
Solution quality estimate total_estimate0.6527
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.646
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17370000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.237; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.112; Smooth: 0.658

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1izna_
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_idd1iznb_
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_idd1iznc_
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_idd1iznd_
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

CATH v4.4 (10 domains)

Domain ID domain_id1iznA01
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_id1iznA02
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_id1iznB01
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_id1iznB02
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_id1iznB03
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily30 — Capz alpha-1 subunit
Domain ID domain_id1iznC01
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_id1iznC02
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_id1iznD01
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_id1iznD02
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_id1iznD03
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily30 — Capz alpha-1 subunit

8. Citations (1)

9. Files and Curves (10)