3CEU

Crystal structure of thiamine phosphate pyrophosphorylase (BT_0647) from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium target BtR268

PDB DOI: https://doi.org/10.2210/pdb3CEU/pdb

Classification: TRANSFERASE
Organism(s): Bacteroides thetaiotaomicron VPI-5482
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2008-02-29 Released: 2008-03-25
Deposition Author(s): Forouhar, F., Chen, Y., Seetharaman, J., Janjua, H., Mao, L., Xiao, R., Foote, E.L., Maglaqui, M., Ciccosanti, C., Zhao, L., Baran, M.C., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.232
R-Value Work: 0.197
R-Value Observed: 0.197

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of thiamine phosphate pyrophosphorylase (BT_0647) from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium target BtR268.

Forouhar, F., Chen, Y., Seetharaman, J., Janjua, H., Mao, L., Xiao, R., Foote, E.L., Maglaqui, M., Ciccosanti, C., Zhao, L., Baran, M.C., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 49.52 kDa
Atom Count: 3,370
Modelled Residue Count: 395
Deposited Residue Count: 420
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Thiamine phosphate pyrophosphorylase	A, B	210	Bacteroides thetaiotaomicron VPI-5482	Mutation(s): 0 Gene Names: BT_0647
UniProt
Find proteins for Q8AA18 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8AA18 Go to UniProtKB: Q8AA18
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8AA18
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: 2.30 Å
R-Value Free: 0.232
R-Value Work: 0.197
R-Value Observed: 0.197
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 46.252	α = 83.88
b = 44.06	β = 62.97
c = 56.041	γ = 86.65

Software Package:

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

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-03-25

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2008-03-25
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2017-10-25
Changes: Refinement description

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.