Cobalt in PDB 1c22: E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex

All present enzymatic activity of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex:
3.4.11.18;

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22 was solved by W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.10 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.128, 67.604, 48.826, 90.00, 111.05, 90.00
R / Rfree (%)	n/a / n/a

The structure of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Sodium	(Na)	1 atom

The binding sites of Cobalt atom in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex (pdb code 1c22). 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: Trifluoromethionine Complex, PDB code: 1c22:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine 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: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:15.5 occ:1.00 OD1 A:ASP108 2.0 13.6 1.0 O A:MF3300 2.0 12.6 1.0 OE1 A:GLU235 2.0 14.1 1.0 OE2 A:GLU204 2.1 12.3 1.0 NE2 A:HIS171 2.1 9.9 1.0 C A:MF3300 2.8 20.6 1.0 CG A:ASP108 3.0 15.4 1.0 CD A:GLU235 3.0 21.0 1.0 CD A:GLU204 3.0 17.4 1.0 CD2 A:HIS171 3.1 12.0 1.0 CE1 A:HIS171 3.1 14.3 1.0 OXT A:MF3300 3.2 15.7 1.0 OE1 A:GLU204 3.3 19.9 1.0 OE2 A:GLU235 3.4 13.7 1.0 CO A:CO402 3.4 15.1 1.0 OD2 A:ASP108 3.5 12.7 1.0 OG1 A:THR202 3.6 11.7 1.0 CG2 A:THR202 3.9 10.1 1.0 CB A:THR202 4.1 8.9 1.0 CA A:MF3300 4.2 13.8 1.0 CB A:ASP108 4.2 11.0 1.0 CG A:HIS171 4.3 9.8 1.0 ND1 A:HIS171 4.3 11.2 1.0 CG A:GLU204 4.3 14.7 1.0 CG A:GLU235 4.4 13.3 1.0 N A:MF3300 4.5 9.9 1.0 O A:HOH603 4.7 45.0 1.0 NE2 A:HIS178 4.8 20.2 1.0 CB A:GLU204 4.9 10.9 1.0

Cobalt binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine 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: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:15.1 occ:1.00 OD2 A:ASP108 2.0 12.7 1.0 OE2 A:GLU235 2.1 13.7 1.0 OD1 A:ASP97 2.1 11.8 1.0 O A:MF3300 2.2 12.6 1.0 N A:MF3300 2.3 9.9 1.0 OD2 A:ASP97 2.3 12.5 1.0 CG A:ASP97 2.5 6.4 1.0 CA A:MF3300 2.9 13.8 1.0 C A:MF3300 2.9 20.6 1.0 CG A:ASP108 3.0 15.4 1.0 CD A:GLU235 3.1 21.0 1.0 OD1 A:ASP108 3.2 13.6 1.0 OE1 A:GLU235 3.4 14.1 1.0 CO A:CO401 3.4 15.5 1.0 O A:HOH504 3.8 13.8 1.0 OG1 A:THR99 3.9 14.2 1.0 CB A:ASP97 4.0 7.1 1.0 OXT A:MF3300 4.1 15.7 1.0 CB A:ASP108 4.3 11.0 1.0 N A:THR109 4.3 7.4 1.0 CB A:MF3300 4.4 20.4 1.0 CG A:GLU235 4.4 13.3 1.0 O A:HOH570 4.4 30.7 1.0 O A:HOH603 4.5 45.0 1.0 O A:VAL98 4.5 14.1 1.0 OE1 A:GLU204 4.6 19.9 1.0 O A:THR109 4.6 11.4 1.0 O A:HOH557 4.6 16.8 1.0 C A:ASP108 4.6 15.0 1.0 CA A:ASP108 4.7 9.9 1.0 OE2 A:GLU204 4.8 12.3 1.0 C A:THR109 4.8 9.5 1.0 CA A:ASP97 4.8 7.6 1.0 N A:VAL98 4.9 8.4 1.0 CB A:GLU235 4.9 6.7 1.0 CA A:THR109 4.9 5.2 1.0 C A:ASP97 4.9 11.0 1.0

W.T.Lowther, Y.Zhang, P.B.Sampson, J.F.Honek, B.W.Matthews. Insights Into the Mechanism of Escherichia Coli Methionine Aminopeptidase From the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues. Biochemistry V. 38 14810 1999.
ISSN: ISSN 0006-2960
PubMed: 10555963
DOI: 10.1021/BI991711G