1ULY

Crystal structure analysis of the ArsR homologue DNA-binding protein from P. horikoshii OT3

PDB DOI: https://doi.org/10.2210/pdb1ULY/pdb

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

Deposited: 2003-09-17 Released: 2004-10-19
Deposition Author(s): Itou, H., Yao, M., Watanabe, N., Tanaka, I.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.268
R-Value Work: 0.204

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of the PH1932 protein, a unique archaeal ArsR type winged-HTH transcription factor from Pyrococcus horikoshii OT3

Itou, H., Yao, M., Watanabe, N., Tanaka, I.

(2008) Proteins 70: 1631-1634

PubMed: 18076033 Search on PubMed
DOI: https://doi.org/10.1002/prot.21851
Primary Citation of Related Structures:
1ULY

Organizational Affiliation

Frontier Research Center for Post-genomic Science and Technology, Hokkaido University, Sapporo 001-0021, Japan.

Macromolecule Content

Total Structure Weight: 23.08 kDa
Atom Count: 1,605
Modelled Residue Count: 190
Deposited Residue Count: 192
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 PH1932	A	192	Pyrococcus horikoshii OT3	Mutation(s): 0 Gene Names: PH1932
UniProt
Find proteins for O59595 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) Explore O59595 Go to UniProtKB: O59595
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O59595
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.268
R-Value Work: 0.204
Space Group: H 3 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 90.64	α = 90
b = 90.64	β = 90
c = 132.26	γ = 120

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2004-10-19

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2004-10-19
Type: Initial release
Version 1.1: 2008-03-28
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance
Version 1.3: 2023-12-27
Changes: Data collection, Database references, Derived calculations

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.