Cobalt in PDB 3mat: E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex

All present enzymatic activity of E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex:
3.4.11.18;

The structure of E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex, PDB code: 3mat was solved by W.T.Lowther, A.M.Orville, D.T.Madden, S.Lim, D.H.Rich, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.80 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.297, 65.155, 51.371, 90.00, 106.12, 90.00
R / Rfree (%)	n/a / n/a

The structure of E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Cobalt atom in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex (pdb code 3mat). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex, PDB code: 3mat:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:17.4 occ:1.00 OD2 A:ASP108 1.9 12.6 1.0 O1 I:AHH1 2.1 19.2 1.0 NE2 A:HIS171 2.2 11.0 1.0 OE2 A:GLU235 2.2 8.9 1.0 OE2 A:GLU204 2.5 9.9 1.0 O2 I:AHH1 2.5 19.3 1.0 CG A:ASP108 2.9 20.7 1.0 C1 I:AHH1 2.9 23.3 1.0 C2 I:AHH1 3.0 20.0 1.0 CE1 A:HIS171 3.1 9.9 1.0 CD A:GLU235 3.1 14.0 1.0 CD2 A:HIS171 3.2 10.8 1.0 CD A:GLU204 3.2 4.9 1.0 OE1 A:GLU204 3.3 16.1 1.0 CO A:CO402 3.3 16.9 1.0 OE1 A:GLU235 3.4 9.8 1.0 OD1 A:ASP108 3.6 3.4 1.0 CA I:AHH1 3.7 23.8 1.0 OG1 A:THR202 3.9 14.8 1.0 CB A:ASP108 4.0 1.7 1.0 N I:ALA2 4.1 22.0 1.0 ND1 A:HIS171 4.3 13.3 1.0 CG2 A:THR202 4.3 13.6 1.0 CG A:HIS171 4.3 13.2 1.0 N I:AHH1 4.3 20.4 1.0 CB A:THR202 4.4 11.8 1.0 NE2 A:HIS178 4.5 16.0 1.0 CG A:GLU204 4.5 7.5 1.0 CG A:GLU235 4.5 7.4 1.0 CE1 A:PHE177 4.8 19.3 1.0 CA I:ALA2 4.9 29.1 1.0

Cobalt binding site 2 out of 2 in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:16.9 occ:1.00 O1 I:AHH1 1.9 19.2 1.0 OD1 A:ASP108 2.1 3.4 1.0 OD1 A:ASP97 2.1 16.8 1.0 OE1 A:GLU235 2.2 9.8 1.0 N I:AHH1 2.3 20.4 1.0 OD2 A:ASP97 2.6 13.3 1.0 CG A:ASP97 2.6 8.9 1.0 C1 I:AHH1 2.8 23.3 1.0 CG A:ASP108 2.9 20.7 1.0 CA I:AHH1 3.1 23.8 1.0 OD2 A:ASP108 3.1 12.6 1.0 CD A:GLU235 3.2 14.0 1.0 CO A:CO401 3.3 17.4 1.0 OE2 A:GLU235 3.4 8.9 1.0 OE1 A:GLU204 4.0 16.1 1.0 OG1 A:THR99 4.0 17.5 1.0 O A:HOH570 4.1 27.5 1.0 CB A:ASP97 4.1 9.8 1.0 C2 I:AHH1 4.1 20.0 1.0 CB A:ASP108 4.2 1.7 1.0 N A:THR109 4.3 11.0 1.0 O A:VAL98 4.3 18.7 1.0 CB I:AHH1 4.4 25.0 1.0 O A:THR109 4.5 9.9 1.0 CG A:GLU235 4.5 7.4 1.0 C A:ASP108 4.5 15.2 1.0 O2 I:AHH1 4.5 19.3 1.0 CA A:ASP108 4.6 10.6 1.0 C A:THR109 4.7 8.0 1.0 O A:HOH504 4.7 23.4 1.0 N A:VAL98 4.7 12.5 1.0 CD A:GLU204 4.8 4.9 1.0 CA A:ASP97 4.8 6.5 1.0 CA A:THR109 4.8 6.1 1.0 C A:ASP97 4.9 17.2 1.0 C A:VAL98 4.9 13.1 1.0 OE2 A:GLU204 4.9 9.9 1.0 CB A:GLU235 5.0 13.7 1.0

W.T.Lowther, A.M.Orville, D.T.Madden, S.Lim, D.H.Rich, B.W.Matthews. Escherichia Coli Methionine Aminopeptidase: Implications of Crystallographic Analyses of the Native, Mutant, and Inhibited Enzymes For the Mechanism of Catalysis. Biochemistry V. 38 7678 1999.
ISSN: ISSN 0006-2960
PubMed: 10387007
DOI: 10.1021/BI990684R