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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: Sun Dec 13 10:38:32 2020

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