1jx2

CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION

Method: X-RAY DIFFRACTION Dmax: 149.8 Å Quality: REASONABLE

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

Myosin-2 heavy chain,Dynamin-A

Dictyostelium discoideum

UniProt P08799

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–765 Fragment:catalytic domain BGC beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;PEG 8000, Tris, potassium chloride, magnesium chloride, glucose, methyl-propane-diol, dithiothreitol, EGTA, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.255

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.

48 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYS2_DICDI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–776; UniProt 3–765

Myosin-2 heavy chain,Dynamin-A

Dictyostelium discoideum

UniProt Q94464

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–316 Fragment:catalytic domain BGC beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;PEG 8000, Tris, potassium chloride, magnesium chloride, glucose, methyl-propane-diol, dithiothreitol, EGTA, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.255

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 DYNA_DICDI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 786–1100; UniProt 2–316

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 1jx2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jx2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jx2
Deposition date deposition_date2001-09-05
Structure title titleCRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION
Keywords keywordsdynamin, GTPase, myosin, fusion-protein, Dictyostelium, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.71
Radius of gyration Rg (electron density) rg_electron42.35
Forward intensity I(0) i0205408000.00
Molecular weight molecular_weight118270.0 kDa
Excluded volume excluded_volume148870 ų
Envelope volume envelope_volume202050 ų
Hydration-shell volume shell_volume44220 ų
Envelope diameter envelope_diameter159.3
Shell Rg shell_rg41.89
Envelope Rg envelope_rg42.46
Shape Rg shape_rg42.30
Total Rg total_rg42.50
Total atoms total_atoms8337
Residues n_residues1039
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 dmax149.8
Rg (real space) rg_real42.30
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real2.0540e+08
I(0) uncertainty (real space) i0_real_error3.4950e+06
Rg (reciprocal space) rg_reciprocal41.71
I(0) (reciprocal space) i0_reciprocal205300000.0000
Solution quality estimate total_estimate0.7487
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.683
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha40090000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.471; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.636; Smooth: 0.680

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1jx2a1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.3 — Myosin S1 fragment, N-terminal domain
Family Family familyb.34.3.1 — Myosin S1 fragment, N-terminal domain
Domain ID domain_idd1jx2a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.9 — Motor proteins
Domain ID domain_idd1jx2a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1jx2a4
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (3 domains)

Domain ID domain_id1jx2A01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily360 — Myosin S1 fragment, N-terminal
Domain ID domain_id1jx2A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology850 — Kinesin
Homologous superfamily homologous superfamily10 — Kinesin motor domain
Domain ID domain_id1jx2A04
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily530

8. Citations (1)

9. Files and Curves (10)