Potassium in PDB 6xlh: Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas

The structure of Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Potassium atom in the Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas (pdb code 6xlh). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas, PDB code: 6xlh:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas within 5.0Å range: probe atom residue distance (Å) B Occ A:K803 b:33.5 occ:1.00 O A:GLY121 3.0 30.5 1.0 O A:ASN92 3.0 34.0 1.0 O A:THR95 3.0 29.9 1.0 O A:LYS98 3.1 30.6 1.0 O1A A:AGS801 3.3 41.6 1.0 OH A:TYR125 3.8 26.6 1.0 C5' A:AGS801 3.9 41.6 1.0 C A:GLY121 4.0 30.5 1.0 C A:ASN92 4.1 34.0 1.0 CE2 A:TYR125 4.1 26.6 1.0 C A:THR95 4.2 29.9 1.0 C A:LYS98 4.2 30.6 1.0 N A:LYS98 4.3 30.6 1.0 CZ A:TYR125 4.3 26.6 1.0 PA A:AGS801 4.5 41.6 1.0 CA A:LEU93 4.5 33.6 1.0 CA A:LYS98 4.6 30.6 1.0 CA A:GLY121 4.6 30.5 1.0 O5' A:AGS801 4.7 41.6 1.0 CB A:LYS98 4.7 30.6 1.0 N A:LEU93 4.7 33.6 1.0 N A:THR95 4.7 29.9 1.0 N A:ALA97 4.8 27.0 1.0 C A:LEU93 4.9 33.6 1.0 CA A:ILE96 4.9 29.5 1.0 O3A A:AGS801 4.9 41.6 1.0 N A:GLY94 4.9 32.9 1.0 N A:ILE96 5.0 29.5 1.0

Potassium binding site 2 out of 2 in the Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Asymmetric Hydrolysis State of HSC82 in Complex with AHA1 Bound with Adp and Atpgammas within 5.0Å range: probe atom residue distance (Å) B Occ B:K803 b:23.9 occ:1.00 O B:GLY121 2.9 30.1 1.0 O B:ASN92 2.9 34.1 1.0 O B:THR95 3.0 27.8 1.0 O2A B:ADP801 3.2 41.6 1.0 O B:LYS98 3.2 30.0 1.0 C5' B:ADP801 3.5 41.6 1.0 OH B:TYR125 3.8 28.8 1.0 CE2 B:TYR125 3.9 28.8 1.0 C B:GLY121 3.9 30.1 1.0 C B:ASN92 4.1 34.1 1.0 C B:THR95 4.1 27.8 1.0 CZ B:TYR125 4.2 28.8 1.0 N B:LYS98 4.2 30.0 1.0 C B:LYS98 4.2 30.0 1.0 O B:LEU93 4.3 33.1 1.0 PA B:ADP801 4.3 41.6 1.0 CA B:LEU93 4.4 33.1 1.0 O5' B:ADP801 4.4 41.6 1.0 N B:ALA97 4.5 24.8 1.0 C B:LEU93 4.5 33.1 1.0 CA B:GLY121 4.5 30.1 1.0 CA B:ILE96 4.6 24.7 1.0 C4' B:ADP801 4.6 41.6 1.0 CA B:LYS98 4.7 30.0 1.0 N B:LEU93 4.7 33.1 1.0 C B:ILE96 4.8 24.7 1.0 CB B:LYS98 4.8 30.0 1.0 N B:ILE96 4.8 24.7 1.0 CD2 B:TYR125 4.9 28.8 1.0 O3A B:ADP801 4.9 41.6 1.0 N B:VAL122 5.0 24.3 1.0

Y.X.Liu, M.Sun, A.G.Myasnikov, D.Elnatan, D.A.Agard. Cryo-Em Structures Reveal A Multistep Mechanism of HSP90 Activation By Co-Chaperone AHA1 To Be Published.