1TDJ

THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI

PDB DOI: https://doi.org/10.2210/pdb1TDJ/pdb

Classification: ALLOSTERY
Organism(s): Escherichia coli
Mutation(s): No

Deposited: 1998-03-27 Released: 1998-10-14
Deposition Author(s): Gallagher, D.T., Gilliland, G.L., Xiao, G., Eisenstein, E.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.340
R-Value Work: 0.200
R-Value Observed: 0.210

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase.

Gallagher, D.T., Gilliland, G.L., Xiao, G., Zondlo, J., Fisher, K.E., Chinchilla, D., Eisenstein, E.

(1998) Structure 6: 465-475

PubMed: 9562556 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(98)00048-3
Primary Citation of Related Structures:
1TDJ

PubMed Abstract:
Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms.

Organizational Affiliation

University of Maryland, Biotechnology Institute, National Institute of Standards and Technology 9600 Gudelsky Drive, Rockville, Maryland 20850, USA. travis@dtg.nist.gov

Macromolecule Content

Total Structure Weight: 56.51 kDa
Atom Count: 3,848
Modelled Residue Count: 494
Deposited Residue Count: 514
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
BIOSYNTHETIC THREONINE DEAMINASE	A	514	Escherichia coli	Mutation(s): 0 EC: 4.2.1.16
UniProt
Find proteins for P04968 (Escherichia coli (strain K12)) Explore P04968 Go to UniProtKB: P04968
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P04968
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PLP Query on PLP Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	PYRIDOXAL-5'-PHOSPHATE C₈ H₁₀ N O₆ P NGVDGCNFYWLIFO-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.340
R-Value Work: 0.200
R-Value Observed: 0.210
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 85.1	α = 90
b = 90.8	β = 90
c = 162.8	γ = 90

Software Package:

Software Name	Purpose
PHASES	phasing
TNT	refinement
XENGEN	data reduction
XENGEN	data scaling

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 1998-10-14

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1998-10-14
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance