2kz7

Solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP)

Method: SOLUTION NMR Dmax: 92.7 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) Leucine-rich repeat-containing protein 16A × 1 (Q6EDY6) SOLUTION NMR NMR measurement conditions:pH 6.5;305 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CARMIL CAH3a/b domain, 0.39 mM [U-2H] CPalpha subunit, 0.39 mM [U-2H] CPbeta subunit, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H; spin labeled at 1 or 5 postions] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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 1–277 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) Leucine-rich repeat-containing protein 16A × 1 (Q6EDY6) SOLUTION NMR NMR measurement conditions:pH 6.5;305 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CARMIL CAH3a/b domain, 0.39 mM [U-2H] CPalpha subunit, 0.39 mM [U-2H] CPbeta subunit, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H; spin labeled at 1 or 5 postions] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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

Leucine-rich repeat-containing protein 16A

Mus musculus

UniProt Q6EDY6

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 965–1039 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) SOLUTION NMR NMR measurement conditions:pH 6.5;305 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CARMIL CAH3a/b domain, 0.39 mM [U-2H] CPalpha subunit, 0.39 mM [U-2H] CPbeta subunit, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.35 mM [U-99% 15N; U-80% 2H] CPalpha subunit, 0.35 mM [U-99% 15N; U-80% 2H] CPbeta subunit, 0.39 mM [U-2H; spin labeled at 1 or 5 postions] CARMIL CAH3a/b domain, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LR16A_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 9–83; UniProt 965–1039

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 2kz7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kz7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kz7
Deposition date deposition_date2010-06-12
Structure title titleSolution structure of the CARMIL CAH3a/b domain bound to capping protein (CP)
Keywords keywordsTROSY, Paramagnetic relaxation enhancement, protein-protein complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier28.59
Radius of gyration Rg (electron density) rg_electron28.22
Forward intensity I(0) i07411320000.00
Molecular weight molecular_weight713140.0 kDa
Excluded volume excluded_volume886070 ų
Envelope volume envelope_volume238660 ų
Hydration-shell volume shell_volume57933 ų
Envelope diameter envelope_diameter106.6
Shell Rg shell_rg42.05
Envelope Rg envelope_rg32.27
Shape Rg shape_rg28.20
Total Rg total_rg28.51
Total atoms total_atoms99730
Residues n_residues6270
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 dmax92.7
Rg (real space) rg_real28.56
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.4110e+09
I(0) uncertainty (real space) i0_real_error1.0400e+08
Rg (reciprocal space) rg_reciprocal28.58
I(0) (reciprocal space) i0_reciprocal7411000000.0000
Solution quality estimate total_estimate0.8927
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.0
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89250000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2kz7a_
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_idd2kz7b_
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 (4 domains)

Domain ID domain_id2kz7A01
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_id2kz7A02
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_id2kz7B01
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_id2kz7B02
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)