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Potassium in PDB 4u6w: Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid

Enzymatic activity of Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid

All present enzymatic activity of Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid:
3.4.11.18;

Protein crystallography data

The structure of Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid, PDB code: 4u6w was solved by T.Arya, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.86 / 1.83
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.149, 77.099, 47.487, 90.00, 91.29, 90.00
R / Rfree (%) 17.6 / 22.4

Other elements in 4u6w:

The structure of Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid (pdb code 4u6w). 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 Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid, PDB code: 4u6w:

Potassium binding site 1 out of 1 in 4u6w

Go back to Potassium Binding Sites List in 4u6w
Potassium binding site 1 out of 1 in the Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Hsmetap (F220M) in Complex with 1-Amino-2-Propylpentyl]Phosphonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K402

b:22.4
occ:1.00
 O A:VAL209 2.5 21.9 1.0
O A:SER363 2.6 18.0 1.0
O A:ASN207 2.8 20.9 1.0
O A:HOH685 2.8 18.2 1.0
O A:SER205 3.0 18.8 1.0
N A:ASN207 3.6 22.8 1.0
C A:ASN207 3.6 22.4 1.0
C A:SER363 3.6 19.7 1.0
C A:VAL209 3.7 17.7 1.0
C A:SER205 3.7 19.6 1.0
C A:VAL206 3.8 19.9 1.0
CA A:ASN207 4.0 21.6 1.0
O A:VAL206 4.1 21.6 1.0
CB A:SER205 4.2 17.0 1.0
N A:VAL209 4.3 20.8 1.0
N A:VAL206 4.3 20.9 1.0
O A:HOH545 4.3 19.6 1.0
N A:SER363 4.4 25.6 1.0
CA A:VAL206 4.4 22.1 1.0
CA A:VAL209 4.4 18.1 1.0
CA A:SER363 4.5 23.1 1.0
CD1 A:ILE225 4.6 24.8 1.0
CG1 A:ILE225 4.6 22.4 1.0
N A:ALA364 4.6 19.4 1.0
CA A:SER205 4.6 15.5 1.0
CB A:SER363 4.7 22.9 1.0
N A:GLU208 4.7 20.5 1.0
N A:ILE210 4.7 18.8 1.0
CA A:ALA364 4.7 18.7 1.0
CB A:VAL209 4.8 18.8 1.0
O A:ILE225 4.8 22.5 1.0
O A:ILE210 4.8 19.2 1.0
C A:GLU208 4.9 22.8 1.0
CA A:ILE210 4.9 19.7 1.0
N A:ASN227 4.9 17.6 1.0
O A:HOH547 5.0 16.8 1.0
CB A:ASN227 5.0 16.5 1.0

Reference:

T.Arya, R.Reddi, C.Kishor, R.J.Ganji, S.Bhukya, R.Gumpena, S.Mcgowan, M.Drag, A.Addlagatta. Identification of the Molecular Basis of Inhibitor Selectivity Between the Human and Streptococcal Type I Methionine Aminopeptidases J.Med.Chem. V. 58 2350 2015.
ISSN: ISSN 0022-2623
PubMed: 25699713
DOI: 10.1021/JM501790E
Page generated: Mon Aug 12 12:12:59 2024

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