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2yuh

Solution structure of the C-terminal region in human tubulin folding cofactor C

Method: SOLUTION NMR Dmax: 69.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tubulin-specific chaperone C

Homo sapiens

UniProt Q15814

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 181–346 Fragment：C-terminal region No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure ambient NMR sample composition：1mM protein, 20mM d-Tris-HCl, 100mM NaCl, 1mM d-DTT, 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 2YUH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2L3L The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin Deposited 2010-09-14 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 26–135（110 aa） Fragment：UNP RESIDUES 26-135
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient
NMR sample composition 0.5-1.0 mM [U-13C; U-15N] TBCC_Nterm-1, 20 mM potassium phosphate-2, 20 mM potassium chloride-3, 1.0 mM TCEP-4, 1.0 mM EDTA-5, 0.05 mM DSS-6, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9M1M Cryo-EM structure of the TBC-DEC-Arl2-alpha-beta-tubulin complex with GDP-AlFx Deposited 2025-02-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 1–346（346 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.21 Å
9M1N Cryo-EM structure of the TBC-DC-Arl2-alpha-beta-tubulin complex with GDP-AlFx Deposited 2025-02-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain C 1–346（346 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.24 Å

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

View Construct and Data Evidence
UniProt name TBCC_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–173； UniProt 181–346

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 2yuh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2yuh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2yuh
Deposition date deposition_date2007-04-06
Structure title titleSolution structure of the C-terminal region in human tubulin folding cofactor C
Keywords keywords;microtubule, beta-tubulin folding, beta-roll, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, CHAPERONE ;; CHAPERONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.52 Å
Radius of gyration Rg (electron density) rg_electron16.75 Å
Forward intensity I(0) i02471580000.00
Molecular weight molecular_weight399560.0 kDa
Excluded volume excluded_volume490230 ų
Envelope volume envelope_volume61171 ų
Hydration-shell volume shell_volume23641 ų
Envelope diameter envelope_diameter76.4 Å
Shell Rg shell_rg29.05 Å
Envelope Rg envelope_rg22.56 Å
Shape Rg shape_rg16.75 Å
Total Rg total_rg16.94 Å
Total atoms total_atoms54760
Residues n_residues3580
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax69.4 Å
Rg (real space) rg_real17.49 Å
Rg uncertainty (real space) rg_real_error0.59 Å
I(0) (real space) i0_real2.4720e+09
I(0) uncertainty (real space) i0_real_error3.4500e+07
Rg (reciprocal space) rg_reciprocal17.49 Å
I(0) (reciprocal space) i0_reciprocal2472000000.0000
Solution quality estimate total_estimate0.7733
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2 Å
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis0.097
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1318000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.419; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.791; Smooth: 1.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2yuhA01
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily70 —
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8. Citations (1)

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9. Files and Curves (10)