5mm7

Ustilago maydis kinesin-5 motor domain with N-terminal extension in the AMPPNP state bound to microtubules

Method: ELECTRON MICROSCOPY Dmax: 115.7 Å Quality: GOOD

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

kinesin-5

Ustilago maydis

UniProt A0A0D1DQH0

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 1–456 Fragment:motor domain, UNP residues 1-456 Tubulin alpha-1A chain × 1 (P02550) Tubulin beta chain × 1 (P02554) MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0D1DQH0_USTMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 2–457; UniProt 1–456

Tubulin alpha-1A chain

Sus scrofa

UniProt P02550

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 1–439 Not recorded kinesin-5 × 1 (A0A0D1DQH0) Tubulin beta chain × 1 (P02554) MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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.

39 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1A_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–439; UniProt 1–439

Tubulin beta chain

Sus scrofa

UniProt P02554

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 1–427 Not recorded kinesin-5 × 1 (A0A0D1DQH0) Tubulin alpha-1A chain × 1 (P02550) MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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.

137 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–427; UniProt 1–427

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 5mm7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5mm7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5mm7
Deposition date deposition_date2016-12-08
Structure title titleUstilago maydis kinesin-5 motor domain with N-terminal extension in the AMPPNP state bound to microtubules
Keywords keywordsUstilago maydis, kinesin-5, motor protein; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.52
Radius of gyration Rg (electron density) rg_electron33.83
Forward intensity I(0) i0330448000.00
Molecular weight molecular_weight141170.0 kDa
Excluded volume excluded_volume174410 ų
Envelope volume envelope_volume229180 ų
Hydration-shell volume shell_volume54419 ų
Envelope diameter envelope_diameter125.8
Shell Rg shell_rg41.90
Envelope Rg envelope_rg34.39
Shape Rg shape_rg33.83
Total Rg total_rg34.39
Total atoms total_atoms9900
Residues n_residues1251
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 dmax115.7
Rg (real space) rg_real34.44
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real3.3040e+08
I(0) uncertainty (real space) i0_real_error5.9240e+06
Rg (reciprocal space) rg_reciprocal34.49
I(0) (reciprocal space) i0_reciprocal330500000.0000
Solution quality estimate total_estimate0.8839
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.2
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha91840000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)