Structure of IDP90540

Tryptophan synthase subunit alpha from Campylobacter jejuni.

Edit deposit information
CSGID target
IDP90540 
PDB Id
3THA (NCBI MMDB
Authors
J.Osipiuk,M.Gu,K.Kwon,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Aug 18, 2011 
Release Date
Aug 31, 2011 

Annotation

Description
Prokaryotic tryptophan synthase, which catalyzes the last processes in the biosynthesis of tryptophan, is a multimeric αββα complex composed of nonidentical α and β subunits. The α and β subunits catalyze different reactions. The α-site cleaves (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate (IGP) to give indole and d-glyceraldehyde 3-phosphate (G3P). The tryptophan-generating β-reaction requires a pyridoxal phosphate cofactor. In order to keep the two reactions in phase, the α-reaction and β-reaction regulate each other through allosteric interactions. Tryptophan synthase subunit alpha is also called as indole-3-glycerol-phosphate lyase. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 31 2 1  
Unit Cell

a=91.97Å, b=91.97Å, c=120.02Å
α=90.00, β=90.00, γ=120.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
43.00-2.37Å (2.43-2.37Å)  
Rall(%)
21.9 
Rwork(%)
21.6 (31.1) 
Rfree(%)
26.3 (37.8) 
Num. observed reflections
24190 (1764) 
Num. Rfree reflections
1233 (85) 
Completeness(%)
99.3 (99.2) 

Model parameters

Num Atoms
3971  
Num Waters
29  
Num Hetatoms
0  
Model mean isotropic B factor
65.980Å2  
RMSD bond length
0.017Å  
RMSD bond angle
1.694°  
Filename uploaded
idp90540.pdb (uploaded on Aug 19, 2011 5:06 PM)  
Inserted
Aug 19, 2011