Sodium 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
Cobalt	(Co)	2 atoms

The binding sites of Sodium atom in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex (pdb code 1c22). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex, PDB code: 1c22:

Sodium binding site 1 out of 1 in the E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of E. Coli Methionine Aminopeptidase: Trifluoromethionine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Na501 b:9.5 occ:1.00 O A:SER231 2.5 15.1 1.0 O A:VAL76 2.7 17.8 1.0 O A:HOH524 2.7 17.5 1.0 O A:ASN74 2.8 16.8 1.0 O A:SER72 3.2 14.5 1.0 C A:SER231 3.7 12.1 1.0 N A:ASN74 3.7 13.3 1.0 C A:ASN74 3.7 18.5 1.0 C A:VAL76 3.9 19.5 1.0 C A:ILE73 3.9 13.3 1.0 C A:SER72 3.9 18.8 1.0 CA A:ASN74 4.0 12.9 1.0 CE A:MET112 4.2 14.6 1.0 O A:ILE73 4.3 15.0 1.0 CB A:SER72 4.3 10.6 1.0 O A:HOH523 4.4 16.2 1.0 CA A:ILE73 4.4 13.7 1.0 N A:ILE73 4.4 14.7 1.0 N A:VAL76 4.4 14.0 1.0 CA A:SER231 4.4 11.2 1.0 CB A:SER231 4.4 15.0 1.0 N A:SER231 4.5 15.1 1.0 O A:ILE93 4.6 17.6 1.0 N A:ALA232 4.6 10.8 1.0 CA A:VAL76 4.7 14.6 1.0 CA A:ALA232 4.7 11.4 1.0 CD1 A:ILE93 4.8 15.5 1.0 CA A:SER72 4.8 10.9 1.0 CG1 A:ILE93 4.8 16.7 1.0 N A:VAL77 4.8 15.0 1.0 N A:GLU75 4.8 11.8 1.0 O A:VAL77 4.9 18.2 1.0 CA A:VAL77 4.9 14.6 1.0 N A:ASN95 4.9 11.5 1.0 C A:GLU75 4.9 18.0 1.0 OG A:SER231 5.0 19.1 1.0 CB A:ASN95 5.0 7.9 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