Atomistry » Cobalt » PDB 2o5s-2r2s » 2os3
Atomistry »
  Cobalt »
    PDB 2o5s-2r2s »
      2os3 »

Cobalt in PDB 2os3: Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes

Enzymatic activity of Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes

All present enzymatic activity of Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes:
3.5.1.88;

Protein crystallography data

The structure of Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes, PDB code: 2os3 was solved by E.E.Kim, K.-H.Kim, J.H.Moon, K.Choi, H.K.Lee, H.S.Parh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.26
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 40.557, 40.557, 217.938, 90.00, 90.00, 120.00
R / Rfree (%) 20.5 / 27.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes (pdb code 2os3). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes, PDB code: 2os3:

Cobalt binding site 1 out of 1 in 2os3

Go back to Cobalt Binding Sites List in 2os3
Cobalt binding site 1 out of 1 in the Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co300

b:41.6
occ:1.00
NE2 A:HIS178 2.2 25.3 1.0
SG A:CYS131 2.3 27.6 1.0
O2 A:BB2400 2.3 43.8 1.0
NE2 A:HIS174 2.4 24.2 1.0
O4 A:BB2400 2.5 48.0 1.0
N1 A:BB2400 2.8 44.0 1.0
C3 A:BB2400 2.9 44.2 1.0
NE2 A:GLN77 3.1 21.6 1.0
CE1 A:HIS178 3.2 24.5 1.0
CD2 A:HIS178 3.2 24.0 1.0
CD2 A:HIS174 3.3 23.6 1.0
CB A:CYS131 3.4 29.3 1.0
CE1 A:HIS174 3.4 23.0 1.0
O A:HOH411 3.6 24.1 1.0
CD A:GLN77 3.8 25.7 1.0
CA A:CYS131 3.9 31.1 1.0
OE1 A:GLN77 4.2 28.5 1.0
C5 A:BB2400 4.3 41.6 1.0
ND1 A:HIS178 4.3 24.6 1.0
CG A:HIS178 4.4 24.8 1.0
O A:HOH403 4.4 30.6 1.0
CG A:HIS174 4.5 22.0 1.0
C6 A:BB2400 4.5 38.2 1.0
ND1 A:HIS174 4.5 25.1 1.0
C A:CYS131 4.7 33.0 1.0
N A:LEU132 4.7 43.6 1.0
O A:GLY130 4.8 37.0 1.0
OE2 A:GLU175 4.8 42.8 1.0
C7 A:BB2400 4.8 34.2 1.0
CG A:GLN77 4.9 28.5 1.0
CD2 A:LEU132 4.9 58.0 1.0

Reference:

E.E.Kim, K.-H.Kim, J.H.Moon, K.Choi, H.K.Lee, H.S.Park. Structures of Actinonin Bound Peptide Deformylases From E. Faecalis and S. Pyogenes To Be Published.
Page generated: Tue Jul 30 15:20:40 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy