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Structure of IDP00538

Crystal Structure of Serine Acetyltransferase CysE from Yersinia pestis

Edit deposit information
CSGID target
IDP00538 
PDB Id
3GVD (NCBI MMDB
Authors
Y.Kim,M.Zhou,S.Peterson,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 30, 2009 
Release Date
May 12, 2009 

Annotation

Description
Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants. Rate-limiting step, abundant O-Acetylserine (thiol) Lyase drive to Cysteine. In the crystal, SAT forms a hexamer with each monomer containing a cysteine molecule in the potential catalytic site. The monomer structure is composed of two distinctive domains, a beta-helix domain and an alpha helix domain. Cysteine molecules were found between two monomers in the alpha-helical regions.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
ACY
PEG
PG5
SO4
GOL

Structure information

Unit cell parameters

Space Group
P 1  
Unit Cell

a=68.47Å, b=81.23Å, c=139.41Å
α=97.07, β=95.32, γ=94.72 
Solvent content
42.95  
Matthews coefficient
2.16  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
45.99-2.40Å (2.43-2.40Å)  
Rall(%)
20.2 
Rwork(%)
19.9 (25.6) 
Rfree(%)
26.4 (29.0) 
Num. observed reflections
117734 (3530) 
Num. Rfree reflections
5945 (182) 
Completeness(%)
97.0 (92.0) 

Model parameters

Num Atoms
25004  
Num Waters
1015  
Num Hetatoms
0  
Model mean isotropic B factor
46.510Å2  
RMSD bond length
0.008Å  
RMSD bond angle
1.160°  
RMSD dihedral angle
17.52°
 
Filename uploaded
dep1w.pdb (uploaded on Mar 30, 2009 11:12 PM)  
Inserted
Mar 30, 2009