3IGX

1.85 Angstrom Resolution Crystal Structure of Transaldolase B (talA) from Francisella tularensis.

PDB DOI: https://doi.org/10.2210/pdb3IGX/pdb

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

Deposited: 2009-07-29 Released: 2009-08-11
Deposition Author(s): Minasov, G., Wawrzak, Z., Skarina, T., Gordon, E., Peterson, S.N., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.85 Å
R-Value Free: 0.186
R-Value Work: 0.150
R-Value Observed: 0.151

wwPDB Validation 3D Report Full Report

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

Literature

1.85 Angstrom Resolution Crystal Structure of Transaldolase B (talA) from Francisella tularensis.

Minasov, G., Wawrzak, Z., Skarina, T., Gordon, E., Peterson, S.N., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecule Content

Total Structure Weight: 72.76 kDa
Atom Count: 6,121
Modelled Residue Count: 642
Deposited Residue Count: 648
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Transaldolase	A, B	324	Francisella tularensis subsp. tularensis SCHU S4	Mutation(s): 0 Gene Names: FTT1093c, FTT_1093c, talA EC: 2.2.1.2
UniProt
Find proteins for Q5NFX0 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NFX0 Go to UniProtKB: Q5NFX0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q5NFX0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PO4 Query on PO4 Download Ideal Coordinates CCD File SDF format, chain D [auth B] SDF format, chain C [auth A] MOL2 format, chain D [auth B] MOL2 format, chain C [auth A] mmCIF format, chain D [auth B] mmCIF format, chain C [auth A]	C [auth A], D [auth B]	PHOSPHATE ION O₄ P NBIIXXVUZAFLBC-UHFFFAOYSA-K		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 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: 1.85 Å
R-Value Free: 0.186
R-Value Work: 0.150
R-Value Observed: 0.151
Space Group: P 2₁ 2₁ 2₁
Diffraction Data: https://doi.org/10.18430/m33igx

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 56.492	α = 90
b = 75.859	β = 90
c = 164.771	γ = 90

Software Package:

Software Name	Purpose
Blu-Ice	data collection
CRANK	phasing
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

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Entry History

Deposition Data

Released Date: 2009-08-11

Deposition Author(s):

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2009-08-11
Type: Initial release
Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.2: 2017-11-01
Changes: Advisory, Refinement description
Version 1.3: 2024-10-16
Changes: Advisory, Data collection, Database references, Derived calculations, Structure summary

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3IGX

1.85 Angstrom Resolution Crystal Structure of Transaldolase B (talA) from Francisella tularensis.

1.85 Angstrom Resolution Crystal Structure of Transaldolase B (talA) from Francisella tularensis.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)