3LYL

Structure of 3-oxoacyl-acylcarrier protein reductase, FabG from Francisella tularensis

PDB DOI: https://doi.org/10.2210/pdb3LYL/pdb

Classification: OXIDOREDUCTASE
Organism(s): Francisella tularensis subsp. tularensis SCHU S4
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2010-02-27 Released: 2010-03-23
Deposition Author(s): Anderson, S.M., Wawrzak, Z., Gordon, E., Hasseman, J., Edwards, A., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.243
R-Value Work: 0.199
R-Value Observed: 0.201

wwPDB Validation 3D Report Full Report

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

Literature

Structure of 3-oxoacyl-acylcarrier protein reductase, FabG from Francisella tularensis

Anderson, S.M., Wawrzak, Z., Gordon, E., Hasseman, J., Edwards, A., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecule Content

Total Structure Weight: 107.6 kDa
Atom Count: 8,140
Modelled Residue Count: 977
Deposited Residue Count: 988
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
3-oxoacyl-(Acyl-carrier-protein) reductase	A, B, C, D	247	Francisella tularensis subsp. tularensis SCHU S4	Mutation(s): 0 Gene Names: fabG, FTT1375, FTT_1375 EC: 1.1.1.100
UniProt
Find proteins for Q5NF68 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NF68 Go to UniProtKB: Q5NF68
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q5NF68
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.243
R-Value Work: 0.199
R-Value Observed: 0.201
Space Group: P 1 2₁ 1
Diffraction Data: https://doi.org/10.18430/M33LYL

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 71.766	α = 90
b = 86.941	β = 98.316
c = 77.522	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
PDB_EXTRACT	data extraction
BLU-MAX	data collection
HKL-2000	data reduction
HKL-2000	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-03-23

Deposition Author(s):

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2010-03-23
Type: Initial release
Version 1.1: 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.