4PNH

Crystal structure of D,D-heptose 1,7-bisphosphate phosphatase from Burkholderia Thailandensis

PDB DOI: https://doi.org/10.2210/pdb4PNH/pdb
Entry: 4PNH supersedes: 4JYR

Classification: HYDROLASE
Organism(s): Burkholderia thailandensis E264
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2014-05-23 Released: 2015-06-24
Deposition Author(s): Kim, M.S., Shin, D.H.
Funding Organization(s): national research foundation of Korea

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.66 Å
R-Value Free: 0.253
R-Value Work: 0.214
R-Value Observed: 0.216

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Crystal structure of D,D-heptose 1,7-bisphosphate phosphatase from Burkholderia Thailandensis

Kim, M.S., Shin, D.H.

To be published.

Macromolecule Content

Total Structure Weight: 256.42 kDa
Atom Count: 13,977
Modelled Residue Count: 1,860
Deposited Residue Count: 2,388
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
D,D-heptose 1,7-bisphosphate phosphatase	A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	199	Burkholderia thailandensis E264	Mutation(s): 0 Gene Names: BTH_I0583 EC: 3.1.3
UniProt
Find proteins for Q2T109 (Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)) Explore Q2T109 Go to UniProtKB: Q2T109
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q2T109
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.66 Å
R-Value Free: 0.253
R-Value Work: 0.214
R-Value Observed: 0.216
Space Group: P 3₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 245.904	α = 90
b = 245.904	β = 90
c = 41.398	γ = 120

Software Package:

Software Name	Purpose
PHENIX	refinement

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2015-06-24

Deposition Author(s):

This entry supersedes: 4JYR

Funding Organization	Location	Grant Number
national research foundation of Korea	Korea, Republic Of	2013R1A1A1A05008769, 2010-0003907

Revision History (Full details and data files)

Version 1.0: 2015-06-24
Type: Initial release
Version 1.1: 2015-07-01
Changes: 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.