3I3W

Structure of a phosphoglucosamine mutase from Francisella tularensis

PDB DOI: https://doi.org/10.2210/pdb3I3W/pdb

Classification: ISOMERASE
Organism(s): Francisella tularensis subsp. tularensis
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2009-07-01 Released: 2010-01-19
Deposition Author(s): Brunzelle, J.S., Wawrzak, Z., Skarina, T., Onopriyenko, O., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.236
R-Value Work: 0.194
R-Value Observed: 0.196

wwPDB Validation 3D Report Full Report

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

Literature

Structure of a phosphoglucosamine mutase from Francisella tularensis

Brunzelle, J.S., Wawrzak, Z., Skarina, T., Onopriyenko, O., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecule Content

Total Structure Weight: 97.42 kDa
Atom Count: 7,026
Modelled Residue Count: 881
Deposited Residue Count: 886
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Phosphoglucosamine mutase	A, B	443	Francisella tularensis subsp. tularensis	Mutation(s): 0 Gene Names: FTT0079, glmM, mrsA EC: 5.4.2.10
UniProt
Find proteins for Q5NII8 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NII8 Go to UniProtKB: Q5NII8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q5NII8
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Modified Residues 2 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET
SEP Query on SEP	A, B	L-PEPTIDE LINKING	C₃ H₈ N O₆ P		SER

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.236
R-Value Work: 0.194
R-Value Observed: 0.196
Space Group: P 2₁ 2₁ 2
Diffraction Data: https://doi.org/10.18430/M33I3W

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 104.43	α = 90
b = 206.68	β = 90
c = 44.76	γ = 90

Software Package:

Software Name	Purpose
BLU-MAX	data collection
PHENIX	model building
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-01-19

Deposition Author(s):

Brunzelle, J.S.

Onopriyenko, O.

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2010-01-19
Type: Initial release
Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.2: 2018-01-24
Changes: 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.