5jx1

The neck-linker and alpha 7 helix of Mus musculus KIF3A fused to EB1

Method: X-RAY DIFFRACTION Dmax: 77.4 Å Quality: REASONABLE

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

Chimera protein of Kinesin-like protein KIF3A and Microtubule-associated protein RP/EB family member 1

Homo sapiens

UniProt P28741

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 352–376 Fragment:UNP P28741 residues 352-376,UNP Q15691 residues 210-257 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;24% (w/v) 2-methyl-2,4-pentanediol (MPD), 10% (w/v) PEG 4000, 100 mM CaCl2, 100 mM (3-(N-morpholino)propanesulfonic acid) (MOPS) pH 7.0, 1 mM CdCl2 Resolution 1.67 Å R-free 0.228

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KIF3A_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–27; UniProt 352–376

Chimera protein of Kinesin-like protein KIF3A and Microtubule-associated protein RP/EB family member 1

Homo sapiens

UniProt Q15691

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 210–257 Fragment:UNP P28741 residues 352-376,UNP Q15691 residues 210-257 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;24% (w/v) 2-methyl-2,4-pentanediol (MPD), 10% (w/v) PEG 4000, 100 mM CaCl2, 100 mM (3-(N-morpholino)propanesulfonic acid) (MOPS) pH 7.0, 1 mM CdCl2 Resolution 1.67 Å R-free 0.228

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.

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

View Construct and Data Evidence
UniProt name MARE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–75; UniProt 210–257

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 5jx1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jx1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5jx1
Deposition date deposition_date2016-05-12
Structure title titleThe neck-linker and alpha 7 helix of Mus musculus KIF3A fused to EB1
Keywords keywordskinesin, coiled-coil, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.56
Radius of gyration Rg (electron density) rg_electron20.91
Forward intensity I(0) i01103980.00
Molecular weight molecular_weight7660.0 kDa
Excluded volume excluded_volume9786 ų
Envelope volume envelope_volume13971 ų
Hydration-shell volume shell_volume7155 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg22.38
Envelope Rg envelope_rg20.96
Shape Rg shape_rg20.87
Total Rg total_rg21.35
Total atoms total_atoms541
Residues n_residues64
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 dmax77.4
Rg (real space) rg_real21.09
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real1.1040e+06
I(0) uncertainty (real space) i0_real_error1.8060e+04
Rg (reciprocal space) rg_reciprocal20.99
I(0) (reciprocal space) i0_reciprocal1104000.0000
Solution quality estimate total_estimate0.6965
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.7
Skewness Skewness skewness0.626
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53400.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.347; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.048; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5jx1a_
Class classa — All alpha proteins
Fold Fold folda.245 — EB1 dimerisation domain-like
Superfamily Superfamily superfamilya.245.1 — EB1 dimerisation domain-like
Family Family familya.245.1.1 — EB1 dimerisation domain-like

8. Citations (1)

9. Files and Curves (10)