5yee

Crystal structure of LokiProfilin1/Rabbit Actin Complex

Method: X-RAY DIFFRACTION Dmax: 90.7 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–377 Not recorded Uncharacterized protein × 1 (A0A0F8V8L2) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;100 mM Hepes, pH 7.0, 20 % w/v Polyethylene glycol 6,000, 200 mM NaCl, 10 mM ATP disodium salt Resolution 1.81 Å R-free 0.249

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 B; PDBConstruct 1–377; UniProt 1–377

Uncharacterized protein

Lokiarchaeum sp. GC14_75

UniProt A0A0F8V8L2

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 1–134 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, HANGING DROP;pH 7;291 K;100 mM Hepes, pH 7.0, 20 % w/v Polyethylene glycol 6,000, 200 mM NaCl, 10 mM ATP disodium salt Resolution 1.81 Å R-free 0.249

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0F8V8L2_9ARCH
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 3–136; UniProt 1–134

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 5yee

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5yee
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5yee
Deposition date deposition_date2017-09-16
Structure title titleCrystal structure of LokiProfilin1/Rabbit Actin Complex
Keywords keywordsActin, Archaea, Lokiarchaea, 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_guinier26.10
Radius of gyration Rg (electron density) rg_electron25.42
Forward intensity I(0) i050828700.00
Molecular weight molecular_weight55554.0 kDa
Excluded volume excluded_volume69604 ų
Envelope volume envelope_volume83756 ų
Hydration-shell volume shell_volume28061 ų
Envelope diameter envelope_diameter93.7
Shell Rg shell_rg32.26
Envelope Rg envelope_rg25.71
Shape Rg shape_rg25.44
Total Rg total_rg26.12
Total atoms total_atoms3896
Residues n_residues495
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 dmax90.7
Rg (real space) rg_real26.16
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real5.0830e+07
I(0) uncertainty (real space) i0_real_error7.7510e+05
Rg (reciprocal space) rg_reciprocal26.14
I(0) (reciprocal space) i0_reciprocal50830000.0000
Solution quality estimate total_estimate0.8643
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis-0.179
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18380000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5yeeb1
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_idd5yeeb2
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 (4 domains)

Domain ID domain_id5yeeB01
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_id5yeeB02
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_id5yeeB03
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_id5yeeB04
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

8. Citations (1)

9. Files and Curves (10)