1fmw

CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II

Method: X-RAY DIFFRACTION Dmax: 102.9 Å Quality: GOOD

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

MYOSIN II HEAVY CHAIN

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–759 Fragment:MOTOR DOMAIN MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;277 K;8% Peg 8000, 50 mM Hepes, 1 mM DTT, pH 7.5, microbatch, temperature 277K Resolution 2.15 Å R-free 0.286

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 1–759; UniProt 1–759

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 1fmw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fmw
Deposition date deposition_date2000-08-18
Structure title titleCRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II
Keywords keywordsmyosin motor domaim, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.02
Radius of gyration Rg (electron density) rg_electron29.39
Forward intensity I(0) i0111407000.00
Molecular weight molecular_weight83423.0 kDa
Excluded volume excluded_volume104370 ų
Envelope volume envelope_volume131300 ų
Hydration-shell volume shell_volume37540 ų
Envelope diameter envelope_diameter109.1
Shell Rg shell_rg36.35
Envelope Rg envelope_rg29.70
Shape Rg shape_rg29.40
Total Rg total_rg30.01
Total atoms total_atoms5885
Residues n_residues738
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 dmax102.9
Rg (real space) rg_real30.08
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.1140e+08
I(0) uncertainty (real space) i0_real_error1.6370e+06
Rg (reciprocal space) rg_reciprocal30.05
I(0) (reciprocal space) i0_reciprocal111400000.0000
Solution quality estimate total_estimate0.8630
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.0
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis-0.103
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20840000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fmwa1
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_idd1fmwa2
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

CATH v4.4 (5 domains)

Domain ID domain_id1fmwA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily360 — Myosin S1 fragment, N-terminal
Domain ID domain_id1fmwA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology850 — Kinesin
Homologous superfamily homologous superfamily10 — Kinesin motor domain
Domain ID domain_id1fmwA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily820
Domain ID domain_id1fmwA04
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily720 — Myosin VI head, motor domain, U50 subdomain
Domain ID domain_id1fmwA05
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)