Cobalt in PDB 1mat: Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme

All present enzymatic activity of Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme:
3.4.11.18;

The structure of Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme, PDB code: 1mat was solved by S.L.Roderick, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.000, 61.700, 54.500, 90.00, 107.30, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Cobalt atom in the Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme (pdb code 1mat). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme, PDB code: 1mat:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:27.4 occ:1.00 OE2 A:GLU204 1.6 19.4 1.0 OD2 A:ASP108 2.0 15.3 1.0 NE2 A:HIS171 2.1 11.4 1.0 OE2 A:GLU235 2.3 23.5 1.0 CD A:GLU204 2.6 0.0 1.0 CO A:CO402 2.9 28.8 1.0 CG A:ASP108 3.0 21.0 1.0 CD2 A:HIS171 3.0 7.9 1.0 OE1 A:GLU204 3.1 31.9 1.0 CE1 A:HIS171 3.3 14.6 1.0 CD A:GLU235 3.3 88.5 1.0 OD1 A:ASP108 3.3 10.5 1.0 OE1 A:GLU235 3.7 24.6 1.0 OG1 A:THR202 3.7 31.0 1.0 CG2 A:THR202 3.8 23.6 1.0 CG A:GLU204 3.8 90.6 1.0 CB A:ASP108 4.2 6.5 1.0 CG A:HIS171 4.2 5.2 1.0 CB A:THR202 4.3 11.8 1.0 ND1 A:HIS171 4.4 11.1 1.0 OD2 A:ASP97 4.5 21.4 1.0 CG A:GLU235 4.6 11.9 1.0 CE1 A:PHE177 4.8 29.9 1.0

Cobalt binding site 2 out of 2 in the Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:28.8 occ:1.00 OD2 A:ASP97 2.0 21.4 1.0 OD1 A:ASP108 2.0 10.5 1.0 OE1 A:GLU235 2.1 24.6 1.0 OD1 A:ASP97 2.2 22.7 1.0 CG A:ASP97 2.4 21.4 1.0 CG A:ASP108 2.8 21.0 1.0 CD A:GLU235 2.9 88.5 1.0 CO A:CO401 2.9 27.4 1.0 OE2 A:GLU235 2.9 23.5 1.0 OD2 A:ASP108 3.1 15.3 1.0 OG1 A:THR99 3.7 24.6 1.0 CB A:ASP97 3.9 13.7 1.0 OE2 A:GLU204 4.0 19.4 1.0 OE1 A:GLU204 4.0 31.9 1.0 O A:HOH505 4.1 16.5 1.0 CD A:GLU204 4.2 0.0 1.0 CB A:ASP108 4.2 6.5 1.0 O A:VAL98 4.3 23.1 1.0 CG A:GLU235 4.3 11.9 1.0 N A:THR109 4.4 17.0 1.0 C A:ASP108 4.6 17.3 1.0 CA A:ASP108 4.7 18.4 1.0 O A:THR109 4.7 20.7 1.0 NE2 A:HIS171 4.9 11.4 1.0 C A:THR109 4.9 15.2 1.0 CA A:THR109 5.0 14.8 1.0 CB A:SER110 5.0 12.9 1.0

S.L.Roderick, B.W.Matthews. Structure of the Cobalt-Dependent Methionine Aminopeptidase From Escherichia Coli: A New Type of Proteolytic Enzyme. Biochemistry V. 32 3907 1993.
ISSN: ISSN 0006-2960
PubMed: 8471602
DOI: 10.1021/BI00066A009