9m1k

Cryo-EM structure of the TBC-DE-Arl2-beta-tubulin complex with GTP

Method: ELECTRON MICROSCOPY Dmax: 136.3 Å Quality: GOOD

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

Tubulin-specific chaperone E

Homo sapiens

UniProt Q15813

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–527 Not recorded Tubulin-specific chaperone D × 1 (Q9BTW9) ADP-ribosylation factor-like protein 2 × 1 (P36404) Tubulin beta chain × 1 (Q767L7) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBCE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–527; UniProt 1–527

Tubulin-specific chaperone D

Homo sapiens

UniProt Q9BTW9

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–1192 Not recorded Tubulin-specific chaperone E × 1 (Q15813) ADP-ribosylation factor-like protein 2 × 1 (P36404) Tubulin beta chain × 1 (Q767L7) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBCD_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–1192; UniProt 1–1192

ADP-ribosylation factor-like protein 2

Homo sapiens

UniProt P36404

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–184 Not recorded Tubulin-specific chaperone E × 1 (Q15813) Tubulin-specific chaperone D × 1 (Q9BTW9) Tubulin beta chain × 1 (Q767L7) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARL2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–184; UniProt 1–184

Tubulin beta chain

Sus scrofa

UniProt Q767L7

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain b; UniProt 1–444 Not recorded Tubulin-specific chaperone E × 1 (Q15813) Tubulin-specific chaperone D × 1 (Q9BTW9) ADP-ribosylation factor-like protein 2 × 1 (P36404) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB5_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain b; PDBConstruct 1–444; UniProt 1–444

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 9m1k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m1k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m1k
Deposition date deposition_date2025-02-26
Structure title titleCryo-EM structure of the TBC-DE-Arl2-beta-tubulin complex with GTP
Keywords keywordschaperone, complex; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.63
Radius of gyration Rg (electron density) rg_electron41.33
Forward intensity I(0) i0613515000.00
Molecular weight molecular_weight203470.0 kDa
Excluded volume excluded_volume254860 ų
Envelope volume envelope_volume339230 ų
Hydration-shell volume shell_volume67828 ų
Envelope diameter envelope_diameter139.4
Shell Rg shell_rg47.38
Envelope Rg envelope_rg40.88
Shape Rg shape_rg41.32
Total Rg total_rg41.68
Total atoms total_atoms14281
Residues n_residues1807
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 dmax136.3
Rg (real space) rg_real41.60
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real6.1350e+08
I(0) uncertainty (real space) i0_real_error1.1790e+07
Rg (reciprocal space) rg_reciprocal41.63
I(0) (reciprocal space) i0_reciprocal613500000.0000
Solution quality estimate total_estimate0.8911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.6
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81840000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)