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Structure of IDP90566

Crystal structure of phosphoserine aminotransferase from Yersinia pestis CO92

Edit deposit information
CSGID target
IDP90566 
PDB Id
3QBO (NCBI MMDB
Authors
B.Nocek,N.Maltseva,L.Papazisi,W.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Boguslaw Nocek 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jan 13, 2011 
Release Date
Feb 09, 2011 

Annotation

Description
Phosphoserine aminotransferases belongs to subgrup IV of the aminotransferaes, catalyses the conversion of O-phospho-L-serine and oxoglutarate to 3-phosphonooxypyruvate and L-glutamate in the major phosphorylated serine biosynthesis pathway. The enzyme requires pyridoxal phosphate as a cofactor, and is part of the aminotransferase class-V family. The cofactor is bound through an aldimine linkage to Lys197 in the active site.  
Functional assignment
 

Ligands

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

Structure information

Unit cell parameters

Space Group
P 21 21 21  
Unit Cell

a=78.34Å, b=87.95Å, c=106.18Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
40.00-2.36Å (2.42-2.36Å)  
Rall(%)
20.0 
Rwork(%)
19.7 (22.5) 
Rfree(%)
26.1 (29.8) 
Num. observed reflections
30591 (2039) 
Num. Rfree reflections
1529 (77) 
Completeness(%)
99.0 (91.2) 

Model parameters

Num Atoms
5801  
Num Waters
185  
Num Hetatoms
0  
Model mean isotropic B factor
26.280Å2  
RMSD bond length
0.018Å  
RMSD bond angle
1.611°  
Filename uploaded
IDP90566-1.pdb (uploaded on Mar 25, 2011 1:55 PM)  
Inserted
Mar 25, 2011