SAXSdb — 1qsd

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

PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR)

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TBCA_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–106； UniProt 1–106 Author chain B； PDBConstruct 1–106； UniProt 1–106

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	1qsd
Deposition date deposition_date	1999-06-21
Structure title title	RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR
Keywords keywords	FOUR-HELIX-BUNDLE, 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.

1qsd__assembly_1__model_1

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

Download this curve (.dat)

1qsd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1qsd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.01 Å
Rg (electron density)	21.45 Å
Total Rg	22.18 Å
Atom count	1682
Residues	204
Excluded volume	29977 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1qsd__assembly_1__model_1`	dimeric （2）	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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1qsda_
Class class	a — All alpha proteins
Fold Fold fold	a.7 — Spectrin repeat-like
Superfamily Superfamily superfamily	a.7.5 — Tubulin chaperone cofactor A
Family Family family	a.7.5.1 — Tubulin chaperone cofactor A

Domain ID domain_id	d1qsdb_
Class class	a — All alpha proteins
Fold Fold fold	a.7 — Spectrin repeat-like
Superfamily Superfamily superfamily	a.7.5 — Tubulin chaperone cofactor A
Family Family family	a.7.5.1 — Tubulin chaperone cofactor A

CATH v4.4 (2 domains)

Domain ID domain_id	1qsdA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	90 —

Domain ID domain_id	1qsdB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	90 —

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Unit-cell length a length_a	45.400 Å
Unit-cell length b length_b	110.100 Å
Unit-cell length c length_c	49.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.20 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2110
R_work r_work	0.2080
R_free r_free	0.2970

Description description	PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR)
Molecular weight formula_weight	12399.0 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1837

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

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

PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR)

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

1qsd__assembly_1__model_1

1qsd__assembly_1__model_1 | I(q)

1qsd__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	155

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

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

PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR)

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

1qsd__assembly_1__model_1

1qsd__assembly_1__model_1 | I(q)

1qsd__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)