4pki

Complex of ATP-actin With the C-terminal Actin-Binding Domain of Tropomodulin

Method: X-RAY DIFFRACTION Dmax: 93.9 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Gelsolin,Tropomodulin-1 chimera × 1 (P06396,P28289) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.25 M sodium chloride, 12% w/v PEG3350 Resolution 2.30 Å R-free 0.201

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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–377; UniProt 1–377

Gelsolin,Tropomodulin-1 chimera

Homo sapiens

UniProt P06396

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 12–136 Fragment:Gelsolin (UNP residues 12-136), GGSGGSGGS linker, Tmod1 Actin-binding site 2 (UNP residues 160-349) Actin, alpha skeletal muscle × 1 (P68135) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.25 M sodium chloride, 12% w/v PEG3350 Resolution 2.30 Å R-free 0.201

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.

60 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GELS_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–125; UniProt 12–136

Gelsolin,Tropomodulin-1 chimera

Homo sapiens

UniProt P28289

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 160–349 Fragment:Gelsolin (UNP residues 12-136), GGSGGSGGS linker, Tmod1 Actin-binding site 2 (UNP residues 160-349) Actin, alpha skeletal muscle × 1 (P68135) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.25 M sodium chloride, 12% w/v PEG3350 Resolution 2.30 Å R-free 0.201

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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TMOD1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 135–324; UniProt 160–349

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 4pki

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pki
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4pki
Deposition date deposition_date2014-05-14
Structure title titleComplex of ATP-actin With the C-terminal Actin-Binding Domain of Tropomodulin
Keywords keywords;Tmod, Actin Filament, Pointed-End Capping Protein, Tropomyosin, Contractile Protein, Actin-binding Protein, Contractile Protein-Actin-Binding Protein complex ;; Contractile Protein/Actin-Binding Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.96
Radius of gyration Rg (electron density) rg_electron28.47
Forward intensity I(0) i093953500.00
Molecular weight molecular_weight76359.0 kDa
Excluded volume excluded_volume95532 ų
Envelope volume envelope_volume114560 ų
Hydration-shell volume shell_volume34055 ų
Envelope diameter envelope_diameter99.1
Shell Rg shell_rg35.34
Envelope Rg envelope_rg28.68
Shape Rg shape_rg28.49
Total Rg total_rg29.05
Total atoms total_atoms10647
Residues n_residues676
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 dmax93.9
Rg (real space) rg_real28.97
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real9.3950e+07
I(0) uncertainty (real space) i0_real_error1.3860e+06
Rg (reciprocal space) rg_reciprocal28.97
I(0) (reciprocal space) i0_reciprocal93950000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20110000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4pkia1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd4pkia2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70

CATH v4.4 (6 domains)

Domain ID domain_id4pkiA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4pkiA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id4pkiA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4pkiA04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id4pkiG01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id4pkiG02
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor

8. Citations (1)

9. Files and Curves (10)