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Potassium in PDB 1yj3: Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis

Enzymatic activity of Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis, PDB code: 1yj3 was solved by A.Addlagatta, M.L.Quillin, O.Omotoso, J.O.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.360, 48.160, 56.540, 90.00, 95.05, 90.00
R / Rfree (%) 20.3 / 24.7

Other elements in 1yj3:

The structure of Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis (pdb code 1yj3). 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 Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis, PDB code: 1yj3:

Potassium binding site 1 out of 1 in 1yj3

Go back to Potassium Binding Sites List in 1yj3
Potassium binding site 1 out of 1 in the Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure Analysis of Product Bound Methionine Aminopeptidase Type 1C From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:14.3
occ:1.00
 O A:ASN109 2.7 15.7 1.0
O A:VAL111 2.7 19.6 1.0
O A:THR265 2.7 10.4 1.0
O A:HOH570 2.7 13.9 1.0
O A:SER107 3.0 13.7 1.0
C A:ASN109 3.6 16.4 1.0
CG2 A:THR265 3.6 15.1 1.0
C A:LEU108 3.7 13.9 1.0
N A:ASN109 3.7 16.5 1.0
O A:LEU108 3.7 13.8 1.0
C A:SER107 3.8 14.2 1.0
C A:THR265 3.8 10.0 1.0
C A:VAL111 3.8 17.6 1.0
CA A:ASN109 4.0 15.0 1.0
N A:VAL111 4.1 16.6 1.0
CB A:SER107 4.2 11.3 1.0
CA A:LEU108 4.3 14.4 1.0
N A:LEU108 4.3 14.3 1.0
N A:THR265 4.4 13.9 1.0
CA A:VAL111 4.5 16.9 1.0
O A:HOH546 4.5 11.5 1.0
CA A:THR265 4.6 10.2 1.0
N A:GLU110 4.6 14.4 1.0
CA A:SER107 4.7 13.2 1.0
N A:ALA266 4.7 9.2 1.0
CB A:THR265 4.7 12.0 1.0
CB A:VAL111 4.7 16.6 1.0
CG1 A:ILE127 4.7 11.3 1.0
C A:GLU110 4.8 15.4 1.0
CA A:ALA266 4.8 9.4 1.0
N A:ILE112 4.8 17.5 1.0
CD1 A:ILE127 4.8 12.3 1.0
O A:HOH512 4.8 8.3 1.0
O A:ILE127 4.8 13.6 1.0
CB A:ASN129 4.9 7.7 1.0
O A:ILE112 5.0 16.9 1.0
N A:ASN129 5.0 11.4 1.0

Reference:

A.Addlagatta, M.L.Quillin, O.Omotoso, J.O.Liu, B.W.Matthews. Identification of An SH3-Binding Motif in A New Class of Methionine Aminopeptidases From Mycobacterium Tuberculosis Suggests A Mode of Interaction with the Ribosome. Biochemistry V. 44 7166 2005.
ISSN: ISSN 0006-2960
PubMed: 15882055
DOI: 10.1021/BI0501176
Page generated: Mon Aug 12 05:50:34 2024

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