2kxp

Solution NMR structure of V-1 bound to capping protein (CP)

Method: SOLUTION NMR Dmax: 91.2 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 7–281 Not recorded F-actin-capping protein subunit beta isoforms 1 and 2 × 1 (P14315) Myotrophin × 1 (P62774) SOLUTION NMR NMR measurement conditions:pH 6.5;305 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] M7C V-1, 90% H2O/10% D2O | 90% H2O/10% 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 1–275; UniProt 7–281

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 2–271 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) Myotrophin × 1 (P62774) SOLUTION NMR NMR measurement conditions:pH 6.5;305 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] M7C V-1, 90% H2O/10% D2O | 90% H2O/10% 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 1–270; UniProt 2–271

Myotrophin

Mus musculus

UniProt P62774

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 1–118 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) 0.1;Pressure ambient NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] V-1, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.35 mM [U-100% 15N; U-99% 2H] capping protein alpha1 subunit, 0.35 mM [U-100% 15N; U-99% 2H] capping protein beta1 subunit, 0.35 mM [U-99% 2H] M7C V-1, 90% H2O/10% D2O | 90% H2O/10% 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.

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

View Construct and Data Evidence
UniProt name MTPN_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–118; 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 2kxp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2kxp
Deposition date deposition_date2010-05-11
Structure title titleSolution NMR structure of V-1 bound to capping protein (CP)
Keywords keywordsprotein-protein interaction, capping protein, V-1, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier29.69
Radius of gyration Rg (electron density) rg_electron29.30
Forward intensity I(0) i08030570000.00
Molecular weight molecular_weight750260.0 kDa
Excluded volume excluded_volume934950 ų
Envelope volume envelope_volume227360 ų
Hydration-shell volume shell_volume55295 ų
Envelope diameter envelope_diameter104.1
Shell Rg shell_rg41.73
Envelope Rg envelope_rg32.37
Shape Rg shape_rg29.27
Total Rg total_rg29.58
Total atoms total_atoms105110
Residues n_residues6630
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 dmax91.2
Rg (real space) rg_real29.63
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real8.0310e+09
I(0) uncertainty (real space) i0_real_error1.1670e+08
Rg (reciprocal space) rg_reciprocal29.66
I(0) (reciprocal space) i0_reciprocal8031000000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39470000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2kxpa_
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_idd2kxpb_
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_idd2kxpc_
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 (6 domains)

Domain ID domain_id2kxpA01
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_id2kxpA02
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_id2kxpB01
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_id2kxpB02
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_id2kxpB03
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_id2kxpC00
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)