3UV1

Crystal structure a major allergen from dust mite

PDB DOI: https://doi.org/10.2210/pdb3UV1/pdb

Classification: ALLERGEN
Organism(s): Dermatophagoides farinae
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2011-11-29 Released: 2012-10-17
Deposition Author(s): Tan, K.W., Kumar, T., Chew, F.T., Mok, Y.K.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.280
R-Value Work: 0.224
R-Value Observed: 0.228

wwPDB Validation 3D Report Full Report

This is version 1.0 of the entry. See complete history.

Literature

Crystal Structure of Der f 7, a Dust Mite Allergen from Dermatophagoides farinae.

Tan, K.W., Jobichen, C., Ong, T.C., Gao, Y.F., Tiong, Y.S., Wong, K.N., Chew, F.T., Sivaraman, J., Mok, Y.K.

(2012) PLoS One 7: e44850-e44850

PubMed: 22970319 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1371/journal.pone.0044850
Primary Citation of Related Structures:
3UV1

PubMed Abstract:
Der f 7 is the group 7 allergen from the dust mite Dermatophagoides farinae, homologous to the major allergen Der p 7 from D. pteronyssinus. Monoclonal antibody that bind to residues Leu48 and Phe50 was found to inhibit IgE binding to residue Asp159, which is important for the cross-reactivity between Der f 7 and Der p 7.

Organizational Affiliation

Department of Biological Sciences, National University of Singapore, Singapore, Singapore.

Macromolecule Content

Total Structure Weight: 44.39 kDa
Atom Count: 3,148
Modelled Residue Count: 380
Deposited Residue Count: 392
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Der f 7 allergen	A, B	196	Dermatophagoides farinae	Mutation(s): 0
UniProt
Find proteins for Q26456 (Dermatophagoides farinae) Explore Q26456 Go to UniProtKB: Q26456
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q26456
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.280
R-Value Work: 0.224
R-Value Observed: 0.228
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 51.092	α = 90
b = 58.234	β = 90
c = 128.978	γ = 90

Software Package:

Software Name	Purpose
ADSC	data collection
PHASER	phasing
PHENIX	refinement
HKL-2000	data reduction
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2012-10-17

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2012-10-17
Type: Initial release

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.