5jvm

The neck-linker and alpha 7 helix of Mus musculus KIF3C

Method: X-RAY DIFFRACTION Dmax: 91.0 Å Quality: REASONABLE

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

Chimera protein of Kinesin-like protein KIF3C and Microtubule-associated protein RP/EB family member 1

Homo sapiens

UniProt O35066

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 374–402 Chain B; UniProt 374–402 Fragment:UNP O35066 residues 374-402,UNP Q15691 residues 207-257 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;30% (w/v) pentaerythritol ethoxylate (PEE) 797, 1.5% (w/v) ethylene glycol monoethylether, 400 mM MgCl2, 100 mM bis-tris propane pH 9.0 Resolution 1.57 Å R-free 0.205

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name KIF3C_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–31; UniProt 374–402 Author chain B; PDBConstruct 3–31; UniProt 374–402

Chimera protein of Kinesin-like protein KIF3C 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 207–257 Chain B; UniProt 207–257 Fragment:UNP O35066 residues 374-402,UNP Q15691 residues 207-257 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;30% (w/v) pentaerythritol ethoxylate (PEE) 797, 1.5% (w/v) ethylene glycol monoethylether, 400 mM MgCl2, 100 mM bis-tris propane pH 9.0 Resolution 1.57 Å R-free 0.205

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 32–82; UniProt 207–257 Author chain B; PDBConstruct 32–82; UniProt 207–257

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 5jvm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5jvm
Deposition date deposition_date2016-05-11
Structure title titleThe neck-linker and alpha 7 helix of Mus musculus KIF3C
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_guinier26.39
Radius of gyration Rg (electron density) rg_electron26.36
Forward intensity I(0) i06470370.00
Molecular weight molecular_weight18902.0 kDa
Excluded volume excluded_volume23643 ų
Envelope volume envelope_volume32039 ų
Hydration-shell volume shell_volume12332 ų
Envelope diameter envelope_diameter91.9
Shell Rg shell_rg28.23
Envelope Rg envelope_rg27.24
Shape Rg shape_rg26.34
Total Rg total_rg26.66
Total atoms total_atoms1330
Residues n_residues161
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 dmax91.0
Rg (real space) rg_real27.05
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real6.4700e+06
I(0) uncertainty (real space) i0_real_error1.1630e+05
Rg (reciprocal space) rg_reciprocal26.85
I(0) (reciprocal space) i0_reciprocal6469000.0000
Solution quality estimate total_estimate0.6710
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.2
Skewness Skewness skewness0.647
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha577200.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.295; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.046; Smooth: 0.792

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5jvma1
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
Domain ID domain_idd5jvma2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5jvmb1
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
Domain ID domain_idd5jvmb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5jvmA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1430
Domain ID domain_id5jvmB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1430

8. Citations (1)

9. Files and Curves (10)