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Cobalt in PDB 2prq: X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica

Enzymatic activity of X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica

All present enzymatic activity of X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica:
3.4.11.10;

Protein crystallography data

The structure of X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica, PDB code: 2prq was solved by P.Munih, A.Moulin, C.C.Stamper, B.Bennet, D.Ringe, G.A.Petsko, R.C.Holz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.15
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 106.200, 106.200, 96.700, 90.00, 90.00, 120.00
R / Rfree (%) 22.4 / 27.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica (pdb code 2prq). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica, PDB code: 2prq:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 2prq

Go back to Cobalt Binding Sites List in 2prq
Cobalt binding site 1 out of 2 in the X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co501

b:32.0
occ:1.00
 NE2 A:HIS256 1.8 31.2 1.0
OD2 A:ASP117 2.0 30.0 1.0
OE2 A:GLU152 2.1 32.7 1.0
O1 A:TRS840 2.2 52.8 1.0
OE1 A:GLU152 2.3 35.0 1.0
CD A:GLU152 2.5 31.5 1.0
CE1 A:HIS256 2.7 31.5 1.0
CG A:ASP117 2.8 30.5 1.0
CD2 A:HIS256 2.9 30.1 1.0
C1 A:TRS840 3.1 53.6 1.0
OD1 A:ASP117 3.1 29.8 1.0
CO A:CO502 3.2 24.3 1.0
O2 A:TRS840 3.4 53.5 1.0
ND1 A:HIS256 3.8 31.0 1.0
C2 A:TRS840 3.9 53.5 1.0
CG A:HIS256 4.0 30.3 1.0
O A:HOH869 4.0 29.7 1.0
CG A:GLU152 4.0 29.4 1.0
C A:TRS840 4.1 52.5 1.0
CB A:ASP117 4.2 28.2 1.0
CE1 A:HIS97 4.2 27.9 1.0
OE1 A:GLU151 4.2 29.9 1.0
NE2 A:HIS97 4.3 28.0 1.0
CD1 A:ILE255 4.7 23.5 1.0
CG2 A:THR101 4.8 28.1 1.0
N A:TRS840 4.8 53.5 1.0
CB A:GLU152 4.9 27.2 1.0

Cobalt binding site 2 out of 2 in 2prq

Go back to Cobalt Binding Sites List in 2prq
Cobalt binding site 2 out of 2 in the X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co502

b:24.3
occ:1.00
 O1 A:TRS840 1.9 52.8 1.0
OD1 A:ASP179 2.0 26.2 1.0
NE2 A:HIS97 2.0 28.0 1.0
OD1 A:ASP117 2.1 29.8 1.0
OD2 A:ASP179 2.2 24.9 1.0
CG A:ASP179 2.4 22.0 1.0
C1 A:TRS840 2.9 53.6 1.0
CE1 A:HIS97 2.9 27.9 1.0
CD2 A:HIS97 3.1 27.1 1.0
CG A:ASP117 3.1 30.5 1.0
CO A:CO501 3.2 32.0 1.0
OD2 A:ASP117 3.4 30.0 1.0
N A:TRS840 3.6 53.5 1.0
OE1 A:GLU151 3.7 29.9 1.0
C A:TRS840 3.8 52.5 1.0
CB A:ASP179 3.9 23.2 1.0
O2 A:TRS840 4.0 53.5 1.0
ND1 A:HIS97 4.1 27.1 1.0
CG A:HIS97 4.2 26.8 1.0
OE2 A:GLU152 4.2 32.7 1.0
OE1 A:GLU152 4.2 35.0 1.0
CD A:GLU151 4.3 29.2 1.0
CB A:ASP118 4.4 27.2 1.0
CD A:GLU152 4.4 31.5 1.0
C2 A:TRS840 4.5 53.5 1.0
CB A:ASP117 4.5 28.2 1.0
OE2 A:GLU151 4.5 31.2 1.0
CG A:MET180 4.5 24.1 1.0
OG A:SER228 4.6 24.9 1.0
C A:ASP117 4.6 28.5 1.0
N A:ASP118 4.6 29.6 1.0
CA A:ASP179 4.7 22.8 1.0
CG A:ASP118 4.7 28.0 1.0
SD A:MET180 4.7 27.0 1.0
CA A:ASP117 4.7 28.0 1.0
OD2 A:ASP118 4.8 29.6 1.0
O A:ASP117 4.9 30.0 1.0
C A:ASP179 4.9 24.4 1.0

Reference:

P.Munih, A.Moulin, C.C.Stamper, B.Bennett, D.Ringe, G.A.Petsko, R.C.Holz. X-Ray Crystallographic Characterization of the Co(II)-Substituted Tris-Bound Form of the Aminopeptidase From Aeromonas Proteolytica. J.Inorg.Biochem. V. 101 1099 2007.
ISSN: ISSN 0162-0134
PubMed: 17574677
DOI: 10.1016/J.JINORGBIO.2007.03.010
Page generated: Tue Jul 30 15:22:22 2024

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