1OIA

U1A rnp domain 1-95

PDB DOI: https://doi.org/10.2210/pdb1OIA/pdb
Entry: 1OIA supersedes: 1NRC

Classification: RIBONUCLEOPROTEIN
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2003-06-12 Released: 2003-06-26
Deposition Author(s): Nagai, K., Evans, P.R.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.242
R-Value Work: 0.192
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal Structure of the RNA-Binding Domain of the U1 Small Nuclear Ribonucleoprotein A

Nagai, K., Oubridge, C., Jessen, T.H., Li, J., Evans, P.R.

(1990) Nature 348: 515

PubMed: 2147232 Search on PubMed
DOI: https://doi.org/10.1038/348515a0
Primary Citation of Related Structures:
1OIA

PubMed Abstract:
The crystal structure of the RNA binding domain of the U1 small nuclear ribonucleoprotein A, which forms part of the ribonucleoprotein complex involved in the excision of introns, has been solved. It contains a four-stranded beta sheet and two alpha helices. The highly conserved segments designated RNP1 and RNP2 lie side by side on the middle two beta strands. U1 RNA binding studies of mutant proteins suggest that the RNA binds to the four-stranded beta sheet and to the flexible loops on one end.

Organizational Affiliation

MRC Laboratory of Molecular Biology, Cambridge, UK.

Macromolecule Content

Total Structure Weight: 21.89 kDa
Atom Count: 1,529
Modelled Residue Count: 176
Deposited Residue Count: 190
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A	A, B	95	Homo sapiens	Mutation(s): 0
UniProt & NIH Common Fund Data Resources
Find proteins for P09012 (Homo sapiens) Explore P09012 Go to UniProtKB: P09012
PHAROS: P09012 GTEx: ENSG00000077312
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P09012
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.242
R-Value Work: 0.192
R-Value Observed: 0.194
Space Group: I 4₁ 3 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 148.125	α = 90
b = 148.125	β = 90
c = 148.125	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
WEIS	data reduction
SCALA	data scaling
MLPHARE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2003-06-26

Deposition Author(s):

This entry supersedes: 1NRC

Revision History (Full details and data files)

Version 1.0: 2003-06-26
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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.