Atomistry » Sodium » PDB 4m04-4mfa » 4mat
Atomistry »
  Sodium »
    PDB 4m04-4mfa »
      4mat »

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

Enzymatic activity of E.Coli Methionine Aminopeptidase HIS79ALA Mutant

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

Protein crystallography data

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

Sodium Binding Sites:

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 4mat

Go back to Sodium Binding Sites List in 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

Reference:

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
Page generated: Mon Oct 7 16:58:38 2024

Last articles

Ca in 5N7D
Ca in 5N5P
Ca in 5N6N
Ca in 5N5K
Ca in 5N5W
Ca in 5N5J
Ca in 5N4L
Ca in 5N3Y
Ca in 5N31
Ca in 5N3V
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy