5hnw

Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state

Method: ELECTRON MICROSCOPY Dmax: 108.0 Å Quality: GOOD

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

Tubulin alpha-1B chain

OrganismNot specified

UniProt P81947

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 2–451 Not recorded Tubulin beta-2B chain × 1 (Q6B856) Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C × 1 (P20480) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.60 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.

249 other PDB entries and 251 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–450; UniProt 2–451

Tubulin beta-2B chain

OrganismNot specified

UniProt Q6B856

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 2–445 Not recorded Tubulin alpha-1B chain × 1 (P81947) Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C × 1 (P20480) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.60 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.

273 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB2B_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–444; UniProt 2–445

Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C

Drosophila melanogaster

UniProt P20480

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 K; UniProt 325–348 Chain K; UniProt 664–700 Fragment:UNP RESIDUES 325-348, 664-700 Tubulin alpha-1B chain × 1 (P81947) Tubulin beta-2B chain × 1 (Q6B856) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.60 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.

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

View Construct and Data Evidence
UniProt name NCD_DROME
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–24; UniProt 325–348 Author chain K; PDBConstruct 335–371; UniProt 664–700

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 5hnw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5hnw
Deposition date deposition_date2016-01-19
Structure title titleStructural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state
Keywords keywordskinesin, kinesin-14, microtubule, ATPase, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.98
Radius of gyration Rg (electron density) rg_electron32.29
Forward intensity I(0) i0284889000.00
Molecular weight molecular_weight132570.0 kDa
Excluded volume excluded_volume164450 ų
Envelope volume envelope_volume200740 ų
Hydration-shell volume shell_volume50120 ų
Envelope diameter envelope_diameter114.9
Shell Rg shell_rg40.51
Envelope Rg envelope_rg32.67
Shape Rg shape_rg32.29
Total Rg total_rg32.87
Total atoms total_atoms9302
Residues n_residues1167
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 dmax108.0
Rg (real space) rg_real32.87
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real2.8490e+08
I(0) uncertainty (real space) i0_real_error4.1930e+06
Rg (reciprocal space) rg_reciprocal32.92
I(0) (reciprocal space) i0_reciprocal284900000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81190000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)