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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 3mat:

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

Cobalt (Co) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor Complex, PDB code: 3mat:

Sodium binding site 1 out of 1 in 3mat

Go back to Sodium Binding Sites List in 3mat
Sodium binding site 1 out of 1 in the E.Coli Methionine Aminopeptidase Transition-State Inhibitor 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 Transition-State Inhibitor Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:28.9
occ:1.00
 O A:SER231 2.5 16.0 1.0
O A:VAL76 2.7 15.9 1.0
O A:HOH521 2.8 17.4 1.0
O A:ASN74 3.1 22.4 1.0
O A:SER72 3.5 19.9 1.0
C A:SER231 3.6 16.5 1.0
N A:ASN74 3.8 19.0 1.0
C A:ASN74 3.9 16.5 1.0
C A:VAL76 3.9 16.6 1.0
C A:ILE73 3.9 19.6 1.0
C A:SER72 4.0 22.4 1.0
CB A:SER72 4.2 14.0 1.0
CA A:ASN74 4.2 18.2 1.0
O A:ILE73 4.2 17.3 1.0
CE A:MET112 4.3 9.2 1.0
N A:ILE73 4.4 18.9 1.0
CA A:ILE73 4.4 19.0 1.0
CA A:SER231 4.4 12.6 1.0
N A:SER231 4.5 13.0 1.0
N A:ALA232 4.5 10.2 1.0
N A:VAL76 4.5 19.1 1.0
O A:HOH537 4.5 14.9 1.0
O A:ILE93 4.6 14.8 1.0
CA A:ALA232 4.6 12.9 1.0
CB A:SER231 4.6 20.7 1.0
CA A:VAL76 4.7 14.6 1.0
CG1 A:ILE93 4.8 12.4 1.0
CA A:SER72 4.8 13.5 1.0
CB A:ASN95 4.8 10.9 1.0
CD1 A:ILE93 4.8 7.2 1.0
N A:ASN95 4.9 10.2 1.0
N A:VAL77 4.9 20.2 1.0
N A:GLU75 4.9 12.5 1.0
CB A:VAL76 5.0 18.9 1.0
O A:HOH515 5.0 22.3 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: Tue Dec 15 06:17:20 2020

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