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Structure of IDP00538

Crystal Structure of Serine Acetyltransferase CysE from Yersinia pestis

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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

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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 sulfate
GOL glycerol

Structure information

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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