4la0

X-ray study of human serum albumin complexed with bicalutamide

Method: X-RAY DIFFRACTION

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

SERUM ALBUMIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	R-BICALUTAMIDE × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	R-BICALUTAMIDE × 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 Author chain B； 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	4la0
Deposition date deposition_date	2013-06-18
Structure title title	X-ray study of human serum albumin complexed with bicalutamide
Keywords keywords	PLASMA PROTEIN, CANCER, ONCOLOGY DRUG COMPLEX, 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.

4la0__assembly_1__model_1

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

Download this curve (.dat)

4la0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4la0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.47 Å
Rg (electron density)	26.47 Å
Total Rg	27.26 Å
Atom count	4652
Residues	581
Excluded volume	82893 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4la0__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4la0__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	SERUM ALBUMIN
Molecular weight formula_weight	66571.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9482

DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL

Entity 2 Entity 2 non-polymer

Description description	R-BICALUTAMIDE
Molecular weight formula_weight	430.4 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	183

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6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d4la0a1
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	d4la0a2
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	d4la0a3
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	d4la0b1
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	d4la0b2
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	d4la0b3
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 (12 domains)

Domain ID domain_id	4la0A01
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	4la0A02
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	4la0A03
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	4la0A04
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	4la0A05
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	4la0A06
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	4la0B01
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	4la0B02
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	4la0B03
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	4la0B04
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	4la0B05
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	4la0B06
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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7. Citations (8)

Structural studies of several clinically important oncology drugs in complex with human serum albumin.

Biochim.Biophys.Acta (2013)

PMID: 23838380 · DOI: 10.1016/j.bbagen.2013.06.032 PRIMARY

Crystallographic survey of albumin drug interaction and preliminary applications in cancer chemotherapy

Burgers medicinal chemistry drug design and development, 7th edition (2010)

DOI: 10.1002/0471266949

Structure of Serum Albumin

Adv.Protein Chem. (1994)

Preliminary crystallographic studies of four crystal forms of serum albumin.

Eur.J.Biochem. (1994)

PMID: 7813459

Erratum. Atomic Structure and Chemistry of Human Serum Albumin

Nature (1993)

Atomic structure and chemistry of human serum albumin.

Nature (1992)

PMID: 1630489 · DOI: 10.1038/358209a0

Structure of Human Serum Albumin

Science (1990)

Three-dimensional structure of human serum albumin.

Science (1989)

PMID: 2727704

Unit-cell length a length_a	56.444 Å
Unit-cell length b length_b	59.568 Å
Unit-cell length c length_c	95.957 Å
Unit-cell angle α angle_alpha	73.22 °
Unit-cell angle β angle_beta	83.93 °
Unit-cell angle γ angle_gamma	74.17 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	29.861 Å
R factor r_factor	0.2018
R_work r_work	0.1994
R_free r_free	0.2540

X-ray study of human serum albumin complexed with bicalutamide

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

4la0__assembly_1__model_1

4la0__assembly_1__model_1 | I(q)

4la0__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) 18 domains

SCOP 2.08 (6 domains)

CATH v4.4 (12 domains)

7. Citations (8)

X-ray study of human serum albumin complexed with bicalutamide

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

4la0__assembly_1__model_1

4la0__assembly_1__model_1 | I(q)

4la0__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) 18 domains

SCOP 2.08 (6 domains)

CATH v4.4 (12 domains)

7. Citations (8)