Annotation

Description

Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of gamma-phosphate from nucleoside triphosphates to nucleoside diphosphates. The subunit folding and the dimeric basic structural unit are remarkably the same for available structures but, depending on species, dimers self-associate to form hexamers or tetramers. NDPK from Campylobacter jejuni has been solved at 2.1 A resolution. Structural analysis strongly supports the oligomerization state of this protein being tetrameric rather than hexameric. 

Functional assignment

 

Structure information

Unit cell parameters

Space Group

P 21 21 21  

Unit Cell

a=85.67Å, b=88.14Å, c=110.92Å
α=90.00, β=90.00, γ=90.00 

Solvent content

63.73  

Matthews coefficient

3.39  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

28.40-2.10Å (2.15-2.10Å)  

R_all(%)

17.1 

R_work(%)

17.0 (19.2) 

R_free(%)

19.2 (20.7) 

Num. observed reflections

49487 (3410) 

Num. R_free reflections

2523 (177) 

Completeness(%)

99.2 (93.4) 

Model parameters

Num Atoms

4297  

Num Waters

328  

Num Hetatoms

391  

Model mean isotropic B factor

38.150Ų  

RMSD bond length

0.017Å  

RMSD bond angle

1.484°  

Filename uploaded

3PJ9.pdb (uploaded on Dec 06, 2010 11:47 AM)  

Inserted

Dec 06, 2010