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Potassium in PDB 2gz5: Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang

Enzymatic activity of Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang

All present enzymatic activity of Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang:
3.4.11.18;

Protein crystallography data

The structure of Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang, PDB code: 2gz5 was solved by A.Addlagatta, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.568, 77.689, 48.644, 90.00, 90.63, 90.00
R / Rfree (%) 13.5 / 14.5

Other elements in 2gz5:

The structure of Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang also contains other interesting chemical elements:

Cobalt (Co) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang (pdb code 2gz5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang, PDB code: 2gz5:

Potassium binding site 1 out of 1 in 2gz5

Go back to Potassium Binding Sites List in 2gz5
Potassium binding site 1 out of 1 in the Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Type 1 Methionine Aminopeptidase in Complex with Ovalicin at 1.1 Ang within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K404

b:14.5
occ:1.00
 O A:HOH828 2.3 44.7 1.0
O A:VAL209 2.6 11.4 1.0
O A:SER363 2.7 12.2 1.0
O A:HOH623 2.8 15.0 1.0
O A:ASN207 2.9 12.1 1.0
O A:SER205 3.0 11.1 1.0
N A:ASN207 3.5 11.8 1.0
C A:VAL206 3.7 10.7 1.0
C A:SER363 3.7 10.4 1.0
C A:SER205 3.7 8.9 1.0
C A:ASN207 3.8 12.0 1.0
C A:VAL209 3.8 9.7 1.0
CA A:ASN207 4.1 11.9 1.0
O A:VAL206 4.1 11.0 1.0
CB A:SER205 4.2 8.8 1.0
N A:VAL206 4.2 9.2 1.0
CA A:VAL206 4.3 10.1 1.0
N A:VAL209 4.3 10.3 1.0
N A:SER363 4.5 11.9 1.0
O A:HOH524 4.5 13.2 1.0
CA A:SER363 4.5 11.0 1.0
CA A:VAL209 4.5 10.0 1.0
CB A:SER363 4.6 12.1 1.0
CA A:SER205 4.6 8.3 1.0
N A:ALA364 4.6 10.3 1.0
CG1 A:ILE225 4.7 12.7 1.0
CA A:ALA364 4.7 9.5 1.0
CD1 A:ILE225 4.8 15.2 1.0
N A:ILE210 4.8 9.9 1.0
O A:ILE225 4.8 11.7 1.0
CB A:VAL209 4.8 10.4 1.0
N A:GLU208 4.8 11.4 1.0
N A:ASN227 4.9 8.2 1.0
C A:GLU208 5.0 10.6 1.0
CB A:ASN227 5.0 8.6 1.0
O A:HOH516 5.0 13.0 1.0

Reference:

A.Addlagatta, B.W.Matthews. Structure of the Angiogenesis Inhibitor Ovalicin Bound to Its Noncognate Target, Human Type 1 Methionine Aminopeptidase. Protein Sci. V. 15 1842 2006.
ISSN: ISSN 0961-8368
PubMed: 16823043
DOI: 10.1110/PS.062278006
Page generated: Mon Aug 12 06:30:18 2024

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