SAXSdb — 4wrn

▼

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

Maltose-binding periplasmic protein,Uromodulin

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ZINC ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	UROM_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 380–695； UniProt 295–610 Author chain B； PDBConstruct 380–695； UniProt 295–610

Maltose-binding periplasmic protein,Uromodulin

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2 其他Polymer 2	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ZINC ION × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MALE_ECO57
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 10–376； UniProt 27–393 Author chain B； PDBConstruct 10–376； UniProt 27–393

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4wrn
Deposition date deposition_date	2014-10-24
Structure title title	Crystal structure of the polymerization region of human uromodulin/Tamm-Horsfall protein
Keywords keywords	ZP DOMAIN, EGF DOMAIN, EXTRACELLULAR MATRIX, GLYCOPROTEIN, structural protein; STRUCTURAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

4wrn__assembly_1__model_1

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

Download this curve (.dat)

4wrn__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4wrn__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	37.08 Å
Rg (electron density)	36.52 Å
Total Rg	36.90 Å
Atom count	20898
Residues	1356
Excluded volume	187990 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4wrn__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Maltose-binding periplasmic protein,Uromodulin
Molecular weight formula_weight	76539.4 kDa
Mutation mutation	;I28T, D108A, K109A, E198A, N199A, A241H, K245H, K265A, A338V, I343V, E385A, E388A, D389A, R393N,R586A, R588A,I28T, D108A, K109A, E198A, N199A, A241H, K245H, K265A, A338V, I343V, E385A, E388A, D389A, R393N,R586A, R588A ;
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	20898

ETGHHHHHHKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEHAFNHGETAMTINGPWAWSNIDTSAVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELVKDPRVAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAGTCEECSIDEDCKSNNGRWHCQCKQDFNITDISLLEHRLECGANDMKVSLGKCQLKSLGFDKVFMYLSDSRCSGFNDRDNRDWVSVVTPARDGPCGTVLTRNETHATYSNTLYLADEIIIRDLNIKINFACSYPLDMKVSLKTALQPMVSALNIRVGGTGMFTVRMALFQTPSYTQPYQGSSVTLSTEAFLYVGTMLDGGDLSRFALLMTNCYATPSSQATDPLKYFIIQDRCPHTRDSTIQVVENGESSQGRFSVQMFRFAGNYDLVYLHCEVYLCDTMNEKCKPTCSGTAFASGSVIDQSRVLNLGPITRKGVQ

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Homo sapiens

Entity 2 Entity 2 branched

Description description	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

▼

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	4wrnA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	4wrnA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	3210 — Zona pellucida, ZP-N domain

Domain ID domain_id	4wrnA03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	4100 — Zona pellucida, ZP-C domain

Domain ID domain_id	4wrnB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	4wrnB02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	3210 — Zona pellucida, ZP-N domain

Domain ID domain_id	4wrnB03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	4100 — Zona pellucida, ZP-C domain

▶

7. Citations (10)

A structured interdomain linker directs self-polymerization of human uromodulin.

Proc.Natl.Acad.Sci.USA (2016)

PMID: 26811476 · DOI: 10.1073/pnas.1519803113 PRIMARY

The rediscovery of uromodulin (Tamm-Horsfall protein): from tubulointerstitial nephropathy to chronic kidney disease.

Kidney Int. (2011)

PMID: 21654721 · DOI: 10.1038/ki.2011.134

Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3.

Cell (2010)

PMID: 20970175 · DOI: 10.1016/j.cell.2010.09.041

Zona pellucida domain proteins.

Annu.Rev.Biochem. (2005)

PMID: 15952882 · DOI: 10.1146/annurev.biochem.74.082803.133039

A duplicated motif controls assembly of zona pellucida domain proteins.

Proc.Natl.Acad.Sci.USA (2004)

PMID: 15079052 · DOI: 10.1073/pnas.0401600101

Tamm-Horsfall glycoprotein: biology and clinical relevance.

Am. J. Kidney Dis. (2003)

PMID: 14520616

The ZP domain is a conserved module for polymerization of extracellular proteins.

Nat.Cell Biol. (2002)

PMID: 12021773 · DOI: 10.1038/ncb802

Mutations in the human alpha-tectorin gene cause autosomal dominant non-syndromic hearing impairment.

Nat.Genet. (1998)

PMID: 9590290 · DOI: 10.1038/ng0598-60

;Isolation of the cDNA encoding glycoprotein-2 (GP-2), the major zymogen granule membrane protein. Homology to uromodulin/Tamm-Horsfall protein. ;

J.Biol.Chem. (1991)

PMID: 1999417

Characterization and separation of an inhibitor of viral hemagglutination present in urine.

Proc. Soc. Exp. Biol. Med. (1950)

PMID: 15430405

Unit-cell length a length_a	242.320 Å
Unit-cell length b length_b	242.320 Å
Unit-cell length c length_c	258.860 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	34.976 Å
R factor r_factor	0.2222
R_work r_work	0.2210
R_free r_free	0.2459

Crystal structure of the polymerization region of human uromodulin/Tamm-Horsfall protein

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

Maltose-binding periplasmic protein,Uromodulin

State in the Current Structure

Other States of the Same Protein in the Database

Maltose-binding periplasmic protein,Uromodulin

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

4wrn__assembly_1__model_1

4wrn__assembly_1__model_1 | I(q)

4wrn__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 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (10)

Crystal structure of the polymerization region of human uromodulin/Tamm-Horsfall protein

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

Maltose-binding periplasmic protein,Uromodulin

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Maltose-binding periplasmic protein,Uromodulin

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

4wrn__assembly_1__model_1

4wrn__assembly_1__model_1 | I(q)

4wrn__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 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (10)