SAXSdb — 1lsh

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

LIPOVITELLIN (LV-1N, LV-1C)

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	di-heneicosanoyl phosphatidyl choline × 7 UNKNOWN BRANCHED FRAGMENT OF PHOSPHOLIPID × 43 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VIT_ICHUN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–1055； UniProt 17–1073 Author chain B； PDBConstruct 1–319； UniProt 1306–1624

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	1lsh
Deposition date deposition_date	2002-05-17
Structure title title	LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN
Keywords keywords	;LIPOVITELLIN, VITELLOGENIN, LIPOPROTEIN, PLASMA APOLIPOPROTE APOLIPOPROTEIN B, APOB, MICROSOMAL TRIGLYCERIDE TRANSFER PR BOUNDARY LIPID, PHOSPHOLIPID STRUCTURE, 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.

1lsh__assembly_1__model_1

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

Download this curve (.dat)

1lsh__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1lsh__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.07 Å
Rg (electron density)	34.69 Å
Total Rg	35.09 Å
Atom count	9426
Residues	1128
Excluded volume	173610 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1lsh__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 (5)

Entity 1 Entity 1 polymer

Description description	LIPOVITELLIN (LV-1N, LV-1C)
Molecular weight formula_weight	117469.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	10935

QFQPGKVYRYSYDAFSISGLPEPGVNRAGLSGEMKIEIHGHTHNQATLKITQVNLKYFLGPWPSDSFYPLTGGYDHFIQQLEVPVRFDYSAGRIGDIYAPPQVTDTAVNIVRGILNLFQLSLKKNQQTFELQETGVEGICQTTYVVQEGYRTNEMAVVKTKDLNNCDHKVYKTMGTAYAERCPTCQKMNKNLRSTAVYNYAIFDEPSGYIIKSAHSEEIQQLSVFDIKEGNVVIESRQKLILEGIQSAPAASQAASLQNRGGLMYKFPSSAITKMSSLFVTKGKNLESEIHTVLKHLVENNQLSVHEDAPAKFLRLTAFLRNVDAGVLQSIWHKLHQQKDYRRWILDAVPAMATSEALLFLKRTLASEQLTSAEATQIVASTLSNQQATRESLSYARELLNTSFIRNRPILRKTAVLGYGSLVFRYCANTVSCPDELLQPLHDLLSQSSDRAKEEEIVLALKALGNAGQPNSIKKIQRFLPGQGKSLDEYSTRVQAEAIMALRNIAKRDPRKVQEIVLPIFLNVAIKSELRIRSCIVFFESKPSVALVSMVAVRLRREPNLQVASFVYSQMRSLSRSSNPEFRDVAAACSVAIKMLGSKLDRLGCRYSKAVHVDTFNARTMAGVSADYFRINSPSGPLPRAVAAKIRGQGMGYASDIVEFGLRAEGLQELLYRGSQEQDAYGTALDRQTLLRSGQARSHVSSIHDTLRKLSDWKSVPEERPLASGYVKVHGQEVVFAELDKKMMQRISQLWHSARSHHAAAQEQIGAVVSKLEQGMDVLLTKGYVVSEVRYMQPVCIGIPMDLNLLVSGVTTNRANLSASFSSLPADMKLADLLATNIELRVAATTSMSQHAVAIMGLTTDLAKAGMQTHYKTSAGLGVNGKIEMNARESNFKASLKPFQQKTVVVLSTMESIVFVRDPSGSRILPVLPPKMTLDKGLISQQQQQPHHQQQPHQHGQDQARAAYQRPWASHEFSPAEQKQIHDIMTARPVMRRKQSCSKSAALSSKVCFSARLRNAAFIRNALLYKITGDYVSKVYVQPTSSKAQITKVELELQAG

Entity 2 Entity 2 polymer

Description description	LIPOVITELLIN (LV-2)
Molecular weight formula_weight	35110.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

KYVPQRKPQTSRRHTPASSSSSSSSSSSSSSSSSSSDSDMTVSAESFEKHSKPKVVIVLRAVRADGKQQGLQTTLYYGLTSNGLPKAKIVAVELSDLSVWKLCAKFRLSAHMKAKAAIGWGKNCQQYRAMLEASTGNLQSHPAARVDIKWGRLPSSLQRAKNALLENGAPVIASKLEMEIMPKANQKHQVSVILAAMTPRRMNIIVKLPKVTYFQQGILLPFTFPSPRFWDRPEGSQSDSLPAQIASAFSGIVQDPVASACELNEQSLTTFNGAFFNYDMPESCYHVLAQECSSRPPFIVLIKLDSERRISLELQLDDK

Entity 3 Entity 3 non-polymer

Description description	di-heneicosanoyl phosphatidyl choline
Molecular weight formula_weight	875.3 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 non-polymer

Description description	UNKNOWN BRANCHED FRAGMENT OF PHOSPHOLIPID
Molecular weight formula_weight	478.9 kDa
Source method src_method	syn
Copy count entity_count	43

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1122

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1lsha1
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.4 — Lipovitellin-phosvitin complex, superhelical domain
Family Family family	a.118.4.1 — Lipovitellin-phosvitin complex, superhelical domain

Domain ID domain_id	d1lsha2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.7 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Superfamily Superfamily superfamily	f.7.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Family Family family	f.7.1.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions

Domain ID domain_id	d1lsha3
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.7 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Superfamily Superfamily superfamily	f.7.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Family Family family	f.7.1.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions

Domain ID domain_id	d1lshb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.7 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Superfamily Superfamily superfamily	f.7.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Family Family family	f.7.1.1 — Lipovitellin-phosvitin complex; beta-sheet shell regions

CATH v4.4 (5 domains)

Domain ID domain_id	1lshA01
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	230 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Homologous superfamily homologous superfamily	10 — Lipovitellin; beta-sheet shell regions, chain A

Domain ID domain_id	1lshA02
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily	20 — Vitellinogen, superhelical

Domain ID domain_id	1lshA03
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	50 — Outer Surface Protein A; domain 2
Homologous superfamily homologous superfamily	20 — Lipovitellin. Chain A, domain 3

Domain ID domain_id	1lshA04
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	80 — Lipovitellin-phosvitin complex, chain A, domain 4
Homologous superfamily homologous superfamily	10 — Lipovitellin-phosvitin complex, chain A, domain 4

Domain ID domain_id	1lshB00
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	90 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Homologous superfamily homologous superfamily	10 — Vitellinogen, beta-sheet shell domain

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Unit-cell length a length_a	190.170 Å
Unit-cell length b length_b	84.520 Å
Unit-cell length c length_c	89.530 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	100.39 °
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	1.900 Å
Low-resolution limit resolution_low	21.600 Å
R factor r_factor	0.1930
R_work r_work	0.1930
R_free r_free	0.2550

LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN

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

LIPOVITELLIN (LV-1N, LV-1C)

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

1lsh__assembly_1__model_1

1lsh__assembly_1__model_1 | I(q)

1lsh__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (4 domains)

CATH v4.4 (5 domains)

7. Citations (2)

LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN

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

LIPOVITELLIN (LV-1N, LV-1C)

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

1lsh__assembly_1__model_1

1lsh__assembly_1__model_1 | I(q)

1lsh__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (4 domains)

CATH v4.4 (5 domains)

7. Citations (2)