7c2f

Crystal Structure of the Thorarchaeota ProGel/rabbit actin complex

Method: X-RAY DIFFRACTION Dmax: 121.9 Å Quality: GOOD

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

Actin, alpha skeletal muscle

Oryctolagus cuniculus

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Gelsolin-like domain-containing protein × 1 (A0A135VMT5) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M MES pH 6.0 0.2 M magnesium chloride hexahydrate 20% w/v polyethylene glycol 6000 Resolution 2.03 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Gelsolin-like domain-containing protein × 1 (A0A135VMT5) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M MES pH 6.0 0.2 M magnesium chloride hexahydrate 20% w/v polyethylene glycol 6000 Resolution 2.03 Å R-free 0.231

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 352 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 1–375; UniProt 3–377 Author chain C; PDBConstruct 1–375; UniProt 3–377

Gelsolin-like domain-containing protein

Candidatus Thorarchaeota archaeon SMTZ1-83

UniProt A0A135VMT5

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 1–92 Not recorded Actin, alpha skeletal muscle × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M MES pH 6.0 0.2 M magnesium chloride hexahydrate 20% w/v polyethylene glycol 6000 Resolution 2.03 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–92 Not recorded Actin, alpha skeletal muscle × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M MES pH 6.0 0.2 M magnesium chloride hexahydrate 20% w/v polyethylene glycol 6000 Resolution 2.03 Å R-free 0.231

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 A0A135VMT5_9ARCH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–94; UniProt 1–92 Author chain D; PDBConstruct 3–94; UniProt 1–92

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 7c2f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7c2f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7c2f
Deposition date deposition_date2020-05-07
Structure title titleCrystal Structure of the Thorarchaeota ProGel/rabbit actin complex
Keywords keywordsactin regulator, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.60
Radius of gyration Rg (electron density) rg_electron34.33
Forward intensity I(0) i0162992000.00
Molecular weight molecular_weight102380.0 kDa
Excluded volume excluded_volume128120 ų
Envelope volume envelope_volume158930 ų
Hydration-shell volume shell_volume41135 ų
Envelope diameter envelope_diameter129.0
Shell Rg shell_rg38.07
Envelope Rg envelope_rg34.43
Shape Rg shape_rg34.34
Total Rg total_rg34.58
Total atoms total_atoms14282
Residues n_residues897
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 dmax121.9
Rg (real space) rg_real34.88
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.6300e+08
I(0) uncertainty (real space) i0_real_error2.8140e+06
Rg (reciprocal space) rg_reciprocal34.71
I(0) (reciprocal space) i0_reciprocal163000000.0000
Solution quality estimate total_estimate0.8350
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.617
Kurtosis Kurtosis kurtosis0.018
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25990000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.714; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.806

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd7c2fa1
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_idd7c2fa2
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_idd7c2fc1
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_idd7c2fc2
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 (2 domains)

Domain ID domain_id7c2fB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7c2fD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin

8. Citations (1)

9. Files and Curves (10)