Sodium in PDB 4mat: E.Coli Methionine Aminopeptidase HIS79ALA Mutant

All present enzymatic activity of E.Coli Methionine Aminopeptidase HIS79ALA Mutant:
3.4.11.18;

The structure of E.Coli Methionine Aminopeptidase HIS79ALA Mutant, PDB code: 4mat 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)	28.80 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.648, 68.298, 55.449, 90.00, 105.98, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Sodium atom in the E.Coli Methionine Aminopeptidase HIS79ALA Mutant (pdb code 4mat). 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 HIS79ALA Mutant, PDB code: 4mat:

Sodium binding site 1 out of 1 in the E.Coli Methionine Aminopeptidase HIS79ALA Mutant


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 HIS79ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Na501 b:16.7 occ:1.00 O A:HOH533 2.2 21.3 1.0 O A:ASN74 2.2 21.8 1.0 O A:VAL76 2.3 19.2 1.0 O A:SER231 2.3 11.7 1.0 C A:ASN74 3.2 19.2 1.0 O A:HOH513 3.2 17.8 1.0 C A:SER231 3.3 14.8 1.0 C A:VAL76 3.4 14.4 1.0 N A:ASN74 3.5 24.3 1.0 CA A:ASN74 3.7 18.5 1.0 N A:SER231 3.8 20.1 1.0 C A:ILE73 3.8 25.9 1.0 N A:VAL76 3.8 19.6 1.0 CA A:SER231 3.8 14.7 1.0 CB A:SER231 3.8 12.6 1.0 O A:SER72 4.0 13.5 1.0 O A:ILE73 4.1 22.7 1.0 CA A:VAL76 4.2 15.0 1.0 N A:GLU75 4.2 16.4 1.0 C A:GLU75 4.3 13.2 1.0 C A:SER72 4.3 21.2 1.0 N A:VAL77 4.4 10.8 1.0 CD1 A:ILE93 4.4 1.0 1.0 O A:HOH514 4.4 13.6 1.0 N A:ALA232 4.4 11.1 1.0 CA A:ILE73 4.5 14.8 1.0 N A:ILE73 4.5 16.4 1.0 CA A:GLU75 4.6 20.1 1.0 CB A:SER72 4.6 15.2 1.0 CA A:VAL77 4.6 14.7 1.0 CB A:VAL76 4.6 14.1 1.0 CG1 A:ILE93 4.7 24.4 1.0 O A:ILE93 4.8 23.1 1.0 CA A:ALA232 4.8 14.3 1.0 CE A:MET112 4.8 16.7 1.0 OG A:SER231 4.8 12.1 1.0 O A:GLU75 5.0 12.9 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