SAXSdb — 5cya

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

Tubulin-specific chaperone C

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 2 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TBCC_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–268； UniProt 1–268 Author chain B； PDBConstruct 1–268； UniProt 1–268

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5cya
Deposition date deposition_date	2015-07-30
Structure title title	Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)
Keywords keywords	;Tubulin cofactors, mirotubule dynamics, tubulin chaperones, Arl2 GTPase-activating protein TBCC, GAP activity, beta helix, beta-sheets, CHAPERONE ;; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5cya__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5cya__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5cya__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	16.61 Å
Rg (electron density)	15.10 Å
Total Rg	16.29 Å
Atom count	1302
Residues	161
Excluded volume	23216 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5cya__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5cya__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Tubulin-specific chaperone C
Molecular weight formula_weight	30750.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2744

MDFTAKIKELERELSETSDYKTLQKKTISLRSELNTLSHSLTSYEKEHFSNDIENVLKSINAKLSESKGKKRLFSFKQKNSSSAVHKNVERTELANAPAYTTTLKKHYVLEKGDSAFENLEFCTVTSTTDYSGNSALSGSLCFRNITKCVINLQRIFFQTGSIFITDCTDSIIFLRSPSDKDFQIRLRDLKNCKILIEKLSPSIDCKQVVIIENCHKCIFNASTRDHLIIQDFSNPFQSEETEDNSAFAFEDFDICNKDTMQLFRAYL

Source Source

Source organism organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Common name common_name	;Baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	93

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Unit-cell length a length_a	69.790 Å
Unit-cell length b length_b	69.790 Å
Unit-cell length c length_c	78.180 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 43
Space-group number int_tables_number	78
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	34.105 Å
R factor r_factor	0.2030
R_work r_work	0.2011
R_free r_free	0.2383

Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)

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

Tubulin-specific chaperone C

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5cya__assembly_1__model_1

5cya__assembly_1__model_1 | I(q)

5cya__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)

Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)

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

Tubulin-specific chaperone C

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5cya__assembly_1__model_1

5cya__assembly_1__model_1 | I(q)

5cya__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)