Calcium in PDB 3n9i: Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92

All present enzymatic activity of Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92:
6.1.1.2;

The structure of Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92, PDB code: 3n9i was solved by B.Nocek, N.Maltseva, L.Papazisi, W.Anderson, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.099, 78.150, 152.176, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.6

The binding sites of Calcium atom in the Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92 (pdb code 3n9i). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92, PDB code: 3n9i:

Calcium binding site 1 out of 1 in the Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca501 b:21.5 occ:0.60 O B:HOH515 2.2 38.8 1.0 O B:HOH516 2.3 29.3 1.0 O B:TYR247 2.3 26.5 1.0 O B:HOH354 2.3 44.4 1.0 O B:HOH487 2.3 46.0 1.0 C B:TYR247 3.5 26.7 1.0 CB B:TYR247 4.4 25.7 1.0 CA B:TYR247 4.4 25.9 1.0 N B:ASP248 4.4 27.1 1.0 OE2 B:GLU274 4.6 24.6 1.0 CA B:ASP248 4.6 29.0 1.0 O B:HOH517 4.6 36.2 1.0 N B:TYR247 4.6 26.1 1.0 CB B:ASP248 4.7 30.0 1.0 CD2 B:TYR247 4.9 29.9 1.0

B.Nocek, N.Maltseva, L.Papazisi, W.Anderson, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of Tryptophanyl-Trna Synthetase From Yersinia Pestis CO92 To Be Published.