SAXSdb — 1hk5

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

SERUM ALBUMIN

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	MYRISTIC ACID × 7 3,5,3',5'-TETRAIODO-L-THYRONINE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ALBU_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–585； UniProt 25–609

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	1hk5
Deposition date deposition_date	2003-03-05
Structure title title	HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) and myristic acid (tetradecanoic acid)
Keywords keywords	PLASMA PROTEIN, HORMONE-BINDING, LIPID-BINDING, THYROXINE, FAMILIAL DYSALBUMINEMIC HYPERTHYROXINEMIA; PLASMA 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.

1hk5__assembly_1__model_1

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

Download this curve (.dat)

1hk5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hk5__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.71 Å
Rg (electron density)	27.85 Å
Total Rg	28.33 Å
Atom count	4596
Residues	582
Excluded volume	82313 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hk5__assembly_1__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 (4)

Entity 1 Entity 1 polymer

Description description	SERUM ALBUMIN
Molecular weight formula_weight	66552.2 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4614

DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVAHLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	PICHIA PASTORIS

Entity 2 Entity 2 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 3 Entity 3 non-polymer

Description description	3,5,3',5'-TETRAIODO-L-THYRONINE
Molecular weight formula_weight	776.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	18

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1hk5a1
Class class	a — All alpha proteins
Fold Fold fold	a.126 — Serum albumin-like
Superfamily Superfamily superfamily	a.126.1 — Serum albumin-like
Family Family family	a.126.1.1 — Serum albumin-like

Domain ID domain_id	d1hk5a2
Class class	a — All alpha proteins
Fold Fold fold	a.126 — Serum albumin-like
Superfamily Superfamily superfamily	a.126.1 — Serum albumin-like
Family Family family	a.126.1.1 — Serum albumin-like

Domain ID domain_id	d1hk5a3
Class class	a — All alpha proteins
Fold Fold fold	a.126 — Serum albumin-like
Superfamily Superfamily superfamily	a.126.1 — Serum albumin-like
Family Family family	a.126.1.1 — Serum albumin-like

CATH v4.4 (6 domains)

Domain ID domain_id	1hk5A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1hk5A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1hk5A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1hk5A04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1hk5A05
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1hk5A06
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	10 —

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Unit-cell length a length_a	190.140 Å
Unit-cell length b length_b	39.040 Å
Unit-cell length c length_c	96.230 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.07 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	38.190 Å
R factor r_factor	0.1990
R_work r_work	0.1990
R_free r_free	0.2590

HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) and myristic acid (tetradecanoic acid)

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

SERUM ALBUMIN

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

1hk5__assembly_1__model_1

1hk5__assembly_1__model_1 | I(q)

1hk5__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)

HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) and myristic acid (tetradecanoic acid)

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

SERUM ALBUMIN

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

1hk5__assembly_1__model_1

1hk5__assembly_1__model_1 | I(q)

1hk5__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)