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Structure of IDP90810

Crystal Structure of FolD Bifunctional Protein from Campylobacter jejuni

Edit deposit information
CSGID target
IDP90810 
PDB Id
3P2O (NCBI MMDB
Authors
Y.Kim,R.Zhang,M.Makowska-Grzyska,L.Papazisi,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Oct 03, 2010 
Release Date
Oct 13, 2010 

Annotation

Description
The interconversion of two major one-carbon donors, methylene and methenyl groups, occurs through the sequential activities of NAD(P)-dependent methylenetetrahydrofolate dehydrogenase (MTHFD) and methenyltetrahydrofolate cyclohydrolase (MTHFC). These activities frequently coexist as a part of a bifunctional enzyme in prokaryotes. In higher organisms, MTHFR and MTHFC are often linked together with another protein, formyl-THF synthetase (FTHFS) and operate as a trifunctional enzyme. The structure of the FolD bifunctional protein, a predicted MTHFR/MTHFC from Campylobacter jejuni with NAD determined to 2.23 A. The structure is a dimer with each subunit consisting of two α/β domains and containing a wide, largely hydrophobic cleft formed between the two domains.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
NAX beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine di nucleotide biological
GOL
MSE modified residue

Structure information

Unit cell parameters

Space Group
C 1 2 1  
Unit Cell

a=134.93Å, b=44.98Å, c=117.02Å
α=90.00, β=119.84, γ=90.00 
Solvent content
50.51  
Matthews coefficient
2.49  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
33.59-2.23Å (2.30-2.23Å)  
Rall(%)
19.3 
Rwork(%)
18.9 (26.0) 
Rfree(%)
25.4 (34.2) 
Num. observed reflections
30855 (2305) 
Num. Rfree reflections
1564 (115) 
Completeness(%)
97.0 (78.0) 

Model parameters

Num Atoms
4274  
Num Waters
105  
Num Hetatoms
199  
Model mean isotropic B factor
62.790Å2  
RMSD bond length
0.010Å  
RMSD bond angle
1.249°  
RMSD dihedral angle
19.73°
 
Filename uploaded
dep.pdb (uploaded on Oct 05, 2010 6:56 AM)  
Inserted
Oct 05, 2010