2E8G

The structure of protein from P. horikoshii at 1.7 angstrom resolution

PDB DOI: https://doi.org/10.2210/pdb2E8G/pdb

Classification: RNA BINDING PROTEIN
Organism(s): Pyrococcus horikoshii OT3
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-01-19 Released: 2008-01-22
Deposition Author(s): Gao, Y.G., Yao, M., Tanaka, I.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.237
R-Value Work: 0.199
R-Value Observed: 0.203

wwPDB Validation 3D Report Full Report

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

Literature

Structure of protein PH0536 from Pyrococcus horikoshii at 1.7 A resolution reveals a novel assembly of an oligonucleotide/oligosaccharide-binding fold and an alpha-helical bundle

Gao, Y.-G., Yao, M., Tanaka, I.

(2008) Proteins 71: 503-508

PubMed: 18186487 Search on PubMed
DOI: https://doi.org/10.1002/prot.21895
Primary Citation of Related Structures:
2E8G

Organizational Affiliation

Faculty of Advanced Life Sciences, Graduate School of Life Sciences, Hokkaido University, Sapporo, Japan.

Macromolecule Content

Total Structure Weight: 53.91 kDa
Atom Count: 4,155
Modelled Residue Count: 480
Deposited Residue Count: 482
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Hypothetical protein PH0536	A, B	241	Pyrococcus horikoshii OT3	Mutation(s): 0 Gene Names: ph0536
UniProt
Find proteins for O58271 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) Explore O58271 Go to UniProtKB: O58271
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O58271
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.237
R-Value Work: 0.199
R-Value Observed: 0.203
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 49.186	α = 90
b = 71.691	β = 96.15
c = 69.193	γ = 90

Software Package:

Software Name	Purpose
HKL-2000	data collection
SOLVE	phasing
REFMAC	refinement
HKL-2000	data reduction
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-01-22

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2008-01-22
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2024-03-13
Changes: Data collection, Database references

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.