SAXSdb — 6hpv

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

Fetuin-B

Mus musculus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACETATE ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FETUB_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–370； UniProt 19–388

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	6hpv
Deposition date deposition_date	2018-09-22
Structure title title	Crystal structure of mouse fetuin-B
Keywords keywords	;Glycoprotein, cystatin domain, fertilization, egg coat, zona pellucida, hardening, metalloprotease inhibitor, ovastacin, ZP2, hydrolase inhibitor, liver-secreted protein ;; hydrolase inhibitor
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.

6hpv__assembly_1__model_1

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

Download this curve (.dat)

6hpv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6hpv__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.68 Å
Rg (electron density)	21.86 Å
Total Rg	22.67 Å
Atom count	4684
Residues	299
Excluded volume	42134 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6hpv__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	Fetuin-B
Molecular weight formula_weight	41954.4 kDa
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	4780

RSPPAPPLPQRPLSPLHPLGCNDSEVLAVAGFALQNINRDQKDGYMLSLNRVHDVREHYQEDMGSLFYLTLDVLETDCHVLSRKAQKDCKPRMFYESVYGQCKAMFHINKPRRVLYLPAYNCTLRPVSKRKTHTTCPDCPSPIDLSNPSALEAATESLAKFNSKSPSKKYELVKVTKAMNQWVSGPAYYVEYLIKEAPCTKSQASCSLQHSDSEPVGICQGSTVQSSLRHVPLIQPVEKSVTVTCEFFESQAQVPGDENPAVTQGPQKLPQKNTAPTSSPSVTAPRGSIQHLPELDDEKPEESKGGSPEEAFPVQLDLTTNPQGDTLDVSFLYLEPGDKKLVVLPFPGKEQRSAECPGPEKENNPLVLPPLEHHHHHH

Source Source

Source organism organism	Mus musculus
Common name common_name	Mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Homo sapiens

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 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	85

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	6hpvA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	10 —

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7. Citations (11)

Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition.

Iucrj (2019)

PMID: 30867929 · DOI: 10.1107/S2052252519001568 PRIMARY

Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases.

Sci Rep (2019)

PMID: 30679641 · DOI: 10.1038/s41598-018-37024-5

Maternal malnourishment induced upregulation of fetuin-B blunts nephrogenesis in the low birth weight neonate.

Dev. Biol. (2018)

PMID: 30189195 · DOI: 10.1016/j.ydbio.2018.09.001

Recombinant fetuin-B protein maintains high fertilization rate in cumulus cell-free mouse oocytes.

Mol. Hum. Reprod. (2017)

PMID: 27733489 · DOI: 10.1093/molehr/gaw067

The novel adipokine/hepatokine fetuin B in severe human and murine diabetic kidney disease.

Diabetes Metab. (2017)

PMID: 28214129 · DOI: 10.1016/j.diabet.2017.01.005

Association of high fetuin-B concentrations in serum with fertilization rate in IVF: a cross-sectional pilot study.

Hum. Reprod. (2016)

PMID: 26759143 · DOI: 10.1093/humrep/dev340

Fetuin B Is a Secreted Hepatocyte Factor Linking Steatosis to Impaired Glucose Metabolism.

Cell Metab. (2015)

PMID: 26603189 · DOI: 10.1016/j.cmet.2015.09.023

Mammalian gamete fusion depends on the inhibition of ovastacin by fetuin-B.

Biol. Chem. (2014)

PMID: 25205729 · DOI: 10.1515/hsz-2014-0189

Fetuin-B, a liver-derived plasma protein is essential for fertilization.

Dev. Cell (2013)

PMID: 23562279 · DOI: 10.1016/j.devcel.2013.03.001

Tissue distribution and activity testing suggest a similar but not identical function of fetuin-B and fetuin-A.

Biochem. J. (2003)

PMID: 12943536 · DOI: 10.1042/BJ20030676

Fetuin-B, a second member of the fetuin family in mammals.

Biochem. J. (2000)

PMID: 10947975 · DOI: 10.1042/bj3500589

Unit-cell length a length_a	67.710 Å
Unit-cell length b length_b	67.710 Å
Unit-cell length c length_c	197.810 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	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	47.878 Å
R factor r_factor	0.2255
R_work r_work	0.2241
R_free r_free	0.2529

Crystal structure of mouse fetuin-B

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

Fetuin-B

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

6hpv__assembly_1__model_1

6hpv__assembly_1__model_1 | I(q)

6hpv__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) 1 domains

CATH v4.4 (1 domains)

7. Citations (11)

Crystal structure of mouse fetuin-B

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

Fetuin-B

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

6hpv__assembly_1__model_1

6hpv__assembly_1__model_1 | I(q)

6hpv__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) 1 domains

CATH v4.4 (1 domains)

7. Citations (11)