1mnd

TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MGADP-ALF4

Method: X-RAY DIFFRACTION Dmax: 94.7 Å Quality: GOOD

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

MYOSIN

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 Mutation:Q760L, R761P, I762N MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.60 Å

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 1mnd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mnd
Deposition date deposition_date1995-04-15
Structure title titleTRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MGADP-ALF4
Keywords keywords;ATPASE, MYOSIN, COILED COIL, ACTIN-BINDING, ATP-BINDING, HEPTAD REPEAT PATTERN, METHYLATION, ALKYLATION, PHOSPHORYLATION, 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_guinier27.75
Radius of gyration Rg (electron density) rg_electron26.92
Forward intensity I(0) i082835300.00
Molecular weight molecular_weight71434.0 kDa
Excluded volume excluded_volume89268 ų
Envelope volume envelope_volume108310 ų
Hydration-shell volume shell_volume33570 ų
Envelope diameter envelope_diameter97.5
Shell Rg shell_rg34.16
Envelope Rg envelope_rg27.42
Shape Rg shape_rg26.93
Total Rg total_rg27.61
Total atoms total_atoms5038
Residues n_residues641
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 dmax94.7
Rg (real space) rg_real27.77
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real8.2840e+07
I(0) uncertainty (real space) i0_real_error1.3590e+06
Rg (reciprocal space) rg_reciprocal27.76
I(0) (reciprocal space) i0_reciprocal82830000.0000
Solution quality estimate total_estimate0.8690
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.0
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.109
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15490000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mnda1
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_idd1mnda2
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 (4 domains)

Domain ID domain_id1mndA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily360 — Myosin S1 fragment, N-terminal
Domain ID domain_id1mndA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily820
Domain ID domain_id1mndA04
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_id1mndA05
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily530

8. Citations (3)

9. Files and Curves (10)