1kk8

SCALLOP MYOSIN (S1-ADP-BeFx) IN THE ACTIN-DETACHED CONFORMATION

Method: X-RAY DIFFRACTION Dmax: 165.8 Å Quality: REASONABLE

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

Myosin Heavy Chain, Striated muscle

OrganismNot specified

UniProt P24733

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–837 Fragment:MYOSIN HEAVY CHAIN Mutation:FRAGMENT: PAPAIN DIGESTED, SUBFRAGMENT 1 (S1) Myosin Regulatory Light Chain, Striated adductor muscle × 1 (P13543) Myosin Essential Light Chain,Striated adductor muscle × 1 (P07291) MG MAGNESIUM ION × 2 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;PEG 20000, magnesium chloride, ethylene glycol, Tris HCl, ADP-berillium floride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.30 Å R-free 0.269

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.

19 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYS_AEQIR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–837; UniProt 1–837

Myosin Regulatory Light Chain, Striated adductor muscle

OrganismNot specified

UniProt P13543

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 13–151 Fragment:MYOSIN REGULATORY LIGHT CHAIN Myosin Heavy Chain, Striated muscle × 1 (P24733) Myosin Essential Light Chain,Striated adductor muscle × 1 (P07291) MG MAGNESIUM ION × 2 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;PEG 20000, magnesium chloride, ethylene glycol, Tris HCl, ADP-berillium floride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.30 Å R-free 0.269

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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLR_AEQIR
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–139; UniProt 13–151

Myosin Essential Light Chain,Striated adductor muscle

OrganismNot specified

UniProt P07291

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–154 Fragment:MYOSIN ESSENTIAL LIGHT CHAIN Myosin Heavy Chain, Striated muscle × 1 (P24733) Myosin Regulatory Light Chain, Striated adductor muscle × 1 (P13543) MG MAGNESIUM ION × 2 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;PEG 20000, magnesium chloride, ethylene glycol, Tris HCl, ADP-berillium floride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.30 Å R-free 0.269

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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLE_AEQIR
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–154; UniProt 1–154

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 1kk8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kk8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kk8
Deposition date deposition_date2001-12-06
Structure title titleSCALLOP MYOSIN (S1-ADP-BeFx) IN THE ACTIN-DETACHED CONFORMATION
Keywords keywordsactin-detached, Myosin, Mechanics of MOTOR, 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_guinier47.00
Radius of gyration Rg (electron density) rg_electron48.79
Forward intensity I(0) i0217601000.00
Molecular weight molecular_weight121180.0 kDa
Excluded volume excluded_volume151690 ų
Envelope volume envelope_volume222720 ų
Hydration-shell volume shell_volume42978 ų
Envelope diameter envelope_diameter175.7
Shell Rg shell_rg45.73
Envelope Rg envelope_rg48.79
Shape Rg shape_rg48.76
Total Rg total_rg48.73
Total atoms total_atoms8517
Residues n_residues1086
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 dmax165.8
Rg (real space) rg_real48.23
Rg uncertainty (real space) rg_real_error2.25
I(0) (real space) i0_real2.1760e+08
I(0) uncertainty (real space) i0_real_error4.6020e+06
Rg (reciprocal space) rg_reciprocal47.01
I(0) (reciprocal space) i0_reciprocal217300000.0000
Solution quality estimate total_estimate0.6796
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.735
Kurtosis Kurtosis kurtosis-0.208
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19180000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.398; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.458; Smooth: 0.180

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1kk8a1
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_idd1kk8a2
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_idd1kk8b_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like
Domain ID domain_idd1kk8c_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

CATH v4.4 (6 domains)

Domain ID domain_id1kk8A02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily360 — Myosin S1 fragment, N-terminal
Domain ID domain_id1kk8A04
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily530
Domain ID domain_id1kk8B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1kk8B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1kk8C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1kk8C02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (2)

9. Files and Curves (10)