To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP90555

Crystal Structure of Tryptophanyl-tRNA Synthetase from Campylobacter jejuni

Edit deposit information
CSGID target
IDP90555 
PDB Id
3M5W (NCBI MMDB
Authors
Y.Kim,M.Zhou,J.Hasseman,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Mar 14, 2010 
Release Date
Mar 31, 2010 

Annotation

Description
This enzyme TrpS catalyzes a two-step reaction, first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA. Among two aminoacyl-tRNA synthetases group, (class I and II), TrpS belongs to class I together with TyrS and forms dimer in the crystal. Each monomer has a N-terminal alpha-beta Rossman fold and a C-terminal alpha-fold. The N-terminal domain interacts with the N-terminal domain of the other chain and the patch formed between the two domains within the chain is for a nucleotide binding. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
SO4
GOL
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=66.15Å, b=50.60Å, c=108.64Å
α=90.00, β=107.61, γ=90.00 
Solvent content
47.66  
Matthews coefficient
2.35  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
47.81-2.32Å (2.40-2.32Å)  
Rall(%)
18.7 
Rwork(%)
18.3 (25.0) 
Rfree(%)
24.3 (34.0) 
Num. observed reflections
31034 (2550) 
Num. Rfree reflections
2135 (169) 
Completeness(%)
96.7 (86.0) 

Model parameters

Num Atoms
5331  
Num Waters
215  
Num Hetatoms
0  
Model mean isotropic B factor
52.790Å2  
RMSD bond length
0.014Å  
RMSD bond angle
1.460°  
RMSD dihedral angle
19.57°
 
Filename uploaded
dep1w.pdb (uploaded on Mar 15, 2010 7:52 AM)  
Inserted
Mar 15, 2010