SAXSdb — 1kgi

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

TRANSTHYRETIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	;3,3',5,5'-TETRAIODOTHYROACETIC ACID ; × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TTHY_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–127； UniProt 21–147 Author chain B； PDBConstruct 1–127； UniProt 21–147 Author chain C； PDBConstruct 1–127； UniProt 21–147 Author chain D； PDBConstruct 1–127； UniProt 21–147

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	1kgi
Deposition date deposition_date	2001-11-27
Structure title title	Rat transthyretin (also called prealbumin) complex with 3,3',5,5'-tetraiodothyroacetic acid (t4ac)
Keywords keywords	PREALBUMIN, TRANSPORT, TETRAIODOTHYROACETIC ACID, THYROID HO, TRANSPORT PROTEIN; TRANSPORT PROTEIN
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.

1kgi__assembly_1__model_1

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

Download this curve (.dat)

1kgi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1kgi__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.25 Å
Rg (electron density)	22.07 Å
Total Rg	22.71 Å
Atom count	3749
Residues	481
Excluded volume	66634 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1kgi__assembly_1__model_1`	tetrameric （4）	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)

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1kgia_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.4 — Transthyretin (synonym: prealbumin)
Family Family family	b.3.4.1 — Transthyretin (synonym: prealbumin)

Domain ID domain_id	d1kgib_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.4 — Transthyretin (synonym: prealbumin)
Family Family family	b.3.4.1 — Transthyretin (synonym: prealbumin)

Domain ID domain_id	d1kgic_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.4 — Transthyretin (synonym: prealbumin)
Family Family family	b.3.4.1 — Transthyretin (synonym: prealbumin)

Domain ID domain_id	d1kgid_
Class class	b — All beta proteins
Fold Fold fold	b.3 — Prealbumin-like
Superfamily Superfamily superfamily	b.3.4 — Transthyretin (synonym: prealbumin)
Family Family family	b.3.4.1 — Transthyretin (synonym: prealbumin)

CATH v4.4 (4 domains)

Domain ID domain_id	1kgiA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	180 — Transthyretin/hydroxyisourate hydrolase domain

Domain ID domain_id	1kgiB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	180 — Transthyretin/hydroxyisourate hydrolase domain

Domain ID domain_id	1kgiC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	180 — Transthyretin/hydroxyisourate hydrolase domain

Domain ID domain_id	1kgiD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	180 — Transthyretin/hydroxyisourate hydrolase domain

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7. Citations (6)

Complex of rat transthyretin with tetraiodothyroacetic acid refined at 2.1 and 1.8 A resolution.

Acta Biochim.Pol. (2001)

PMID: 11995998 PRIMARY

;Structure of New Polymorphic Monoclinic Form of Hum Transthyretin at 3A Resolution Reveals a Mixed Comp between Unliganded and T4-Bound Tetramers of Ttr ;

Acta Crystallogr.,Sect.D (2001)

DOI: 10.1107/S0907444901006047

;STRUCTURE OF RAT (rTTR) TRANSTHYRETIN COMPLEX WITH THYROXINE AT 2.5 A RESOLUTION: FIRST NON-BIASED INS INTO THYROXINE BINDING REVEALS DIFFERENT HORMONE ORIENTATION IN TWO BINDING SITES ;

Acta Crystallogr.,Sect.D (2001)

DOI: 10.1107/S0907444901007235

;Structures of Human Transthyretin Complexed with Thyroxine at 2.0 A Resolution and 3',5'-Dinitro-N-Acetyl-L-Thyronine at 2.2 A Resolution ;

Acta Crystallogr.,Sect.D (1996)

DOI: 10.1107/S0907444996003046

;Structural Aspects of Inotropic Bipyridine Binding. Crystal Structure Determination to 1.9 A of the Human Serum Transthyretin-Milrinone Complex ;

J.Biol.Chem. (1993)

;Mechanism of Molecular Recognition. Structural Aspects of 3,3'-Diiodo-L-Thyronine Binding to Human Serum Transthyretin ;

J.Biol.Chem. (1992)

Unit-cell length a length_a	81.510 Å
Unit-cell length b length_b	81.510 Å
Unit-cell length c length_c	160.238 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	32

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2040
R_work r_work	0.2070
R_free r_free	0.2400

Description description	TRANSTHYRETIN
Molecular weight formula_weight	13614.1 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4106

Rat transthyretin (also called prealbumin) complex with 3,3',5,5'-tetraiodothyroacetic acid (t4ac)

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

TRANSTHYRETIN

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

1kgi__assembly_1__model_1

1kgi__assembly_1__model_1 | I(q)

1kgi__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

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (6)

Description description	;3,3',5,5'-TETRAIODOTHYROACETIC ACID ;
Molecular weight formula_weight	747.8 kDa
Source method src_method	syn
Copy count entity_count	2

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	281

Rat transthyretin (also called prealbumin) complex with 3,3',5,5'-tetraiodothyroacetic acid (t4ac)

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

TRANSTHYRETIN

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

1kgi__assembly_1__model_1

1kgi__assembly_1__model_1 | I(q)

1kgi__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

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (6)