Potassium in PDB 7d23: Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site

All present enzymatic activity of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site:
2.3.2.5;

The structure of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site, PDB code: 7d23 was solved by K.-F.Huang, J.-S.Huang, M.-L.Wu, W.-L.Hsieh, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.00 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.471, 71.2, 80.092, 90, 90, 90
R / Rfree (%)	16 / 18.6

The binding sites of Potassium atom in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site (pdb code 7d23). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site, PDB code: 7d23:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:K401 b:7.1 occ:1.00 O3 A:TRS403 2.1 12.7 0.6 OE2 A:GLU184 2.1 11.2 1.0 NE2 A:HIS322 2.2 11.1 1.0 OD2 A:ASP144 2.2 9.8 1.0 O2 A:TRS403 2.5 15.7 1.0 C3 A:TRS403 2.5 10.9 1.0 OE1 A:GLU184 2.8 12.8 1.0 CD A:GLU184 2.8 10.3 1.0 CG A:ASP144 3.0 9.1 1.0 OD1 A:ASP144 3.0 9.6 1.0 CD2 A:HIS322 3.2 10.6 1.0 CE1 A:HIS322 3.2 12.0 1.0 C2 A:TRS403 3.4 13.0 1.0 C A:TRS403 3.6 11.2 1.0 O A:HOH539 4.1 10.4 1.0 NE1 A:TRP321 4.1 11.4 1.0 OE1 A:GLU183 4.2 14.9 1.0 CG A:GLU184 4.3 9.8 1.0 ND1 A:HIS322 4.3 12.2 1.0 CG A:HIS322 4.3 10.7 1.0 CB A:ASP144 4.4 8.2 1.0 N A:TRS403 4.5 16.2 1.0 C1 A:TRS403 4.6 12.7 1.0 NE2 A:HIS128 4.6 8.7 1.0 O1 A:TRS403 4.7 15.8 1.0 O A:HOH520 4.8 14.2 1.0 CE2 A:TRP321 4.8 11.1 1.0 O A:HOH549 4.8 9.0 1.0 CD2 A:LEU239 4.9 9.3 1.0 CD1 A:TRP321 4.9 11.4 1.0 CE1 A:HIS128 4.9 8.4 1.0 CZ2 A:TRP321 5.0 11.8 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with One K Ion Bound to the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:23.8 occ:1.00 O A:HOH817 2.4 32.3 1.0 O A:HOH800 2.4 30.1 1.0 O A:HOH808 2.4 32.1 1.0 O A:HOH813 2.5 36.8 1.0 O A:HOH889 2.5 40.4 1.0 NE2 A:HIS40 2.6 14.1 1.0 CE1 A:HIS40 3.5 13.9 1.0 CD2 A:HIS40 3.6 13.7 1.0 O A:HOH891 4.4 41.5 1.0 O A:HOH727 4.6 23.8 1.0 ND1 A:HIS40 4.7 13.8 1.0 CG A:HIS40 4.8 12.7 1.0 O A:HOH519 4.9 20.7 1.0

K.F.Huang, J.S.Huang, M.L.Wu, W.L.Hsieh, K.C.Hsu, H.L.Hsu, T.P.Ko, A.H-J Wang. A Unique Carboxylic-Acid Hydrogen-Bond Network (Cahbn) Confers Glutaminyl Cyclase Activity on M28 Family Enzymes. J.Mol.Biol. 66960 2021.
ISSN: ESSN 1089-8638
PubMed: 33774034
DOI: 10.1016/J.JMB.2021.166960