SAXSdb — 1zi7

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

KES1 protein

Saccharomyces cerevisiae

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	SULFATE ION × 2 water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	SULFATE ION × 2 water × 1	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 3	SULFATE ION × 6 water × 3	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 4 water × 2	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	KES1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–406； UniProt 30–434 Author chain B； PDBConstruct 5–406； UniProt 30–434 Author chain C； PDBConstruct 5–406； UniProt 30–434

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	1zi7
Deposition date deposition_date	2005-04-27
Structure title title	Structure of truncated yeast oxysterol binding protein Osh4
Keywords keywords	oxysterol, sterol binding protein, LIPID BINDING PROTEIN; LIPID BINDING 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.

1zi7__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1zi7__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1zi7__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	22.69 Å
Rg (electron density)	21.48 Å
Total Rg	22.59 Å
Atom count	3233
Residues	398
Excluded volume	57598 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1zi7__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1zi7__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1zi7__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1zi7__assembly_4__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1zi7__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1zi7__assembly_6__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 (3)

Entity 1 Entity 1 polymer

Description description	KES1 protein
Molecular weight formula_weight	46491.6 kDa
Mutation mutation	236RGYFS -> VD
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	9873

GAMDPPFILSPISLTEFSQYWAEHPELFLEPSFINDDNYKEHCLIDPEVESPELARMLAVTKWFISTLKSQYCSRNESLGSEKKPLNPFLGELFVGKWENKEHPEFGETVLLSEQVSHHPPVTAFSIFNDKNKVKLQGYNQIKASFTKSLMLTVKQFGHTMLDIKDESYLVTPPPLHIEGILVASPFVELEGKSYIQSSTGLLCVIEFSGVDGKKNSFKARIYKDSKDSKDKEKALYTISGQWSGSSKIIKANKKEESRLFYDAARIPAEHLNVKPLEEQHPLESRKAWYDVAGAIKLGDFNLIAKTKTELEETQRELRKEEEAKGISWQRRWFKDFDYSVTPEEGALVPEKDDTFLKLASALNLSTKNAPSGTLVGDKEDRKEDLSSIHWRFQRELWDEEKEIVL

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	Escherichia coli BL21(DE3)

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	6

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	141

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1zi7a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.338 — Oxysterol-binding protein-like
Superfamily Superfamily superfamily	d.338.1 — Oxysterol-binding protein-like
Family Family family	d.338.1.1 — Oxysterol-binding protein

Domain ID domain_id	d1zi7b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.338 — Oxysterol-binding protein-like
Superfamily Superfamily superfamily	d.338.1 — Oxysterol-binding protein-like
Family Family family	d.338.1.1 — Oxysterol-binding protein

Domain ID domain_id	d1zi7c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.338 — Oxysterol-binding protein-like
Superfamily Superfamily superfamily	d.338.1 — Oxysterol-binding protein-like
Family Family family	d.338.1.1 — Oxysterol-binding protein

CATH v4.4 (3 domains)

Domain ID domain_id	1zi7A02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1150 —

Domain ID domain_id	1zi7B02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1150 —

Domain ID domain_id	1zi7C02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	1150 —

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Unit-cell length a length_a	93.903 Å
Unit-cell length b length_b	100.853 Å
Unit-cell length c length_c	117.624 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.53 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	45.110 Å
R factor r_factor	0.2100
R_work r_work	0.2100
R_free r_free	0.2460

Structure of truncated yeast oxysterol binding protein Osh4

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

KES1 protein

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

1zi7__assembly_2__model_1

1zi7__assembly_2__model_1 | I(q)

1zi7__assembly_2__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

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Structure of truncated yeast oxysterol binding protein Osh4

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

KES1 protein

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

1zi7__assembly_2__model_1

1zi7__assembly_2__model_1 | I(q)

1zi7__assembly_2__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

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)