Potassium in PDB 2vqw: Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR)

All present enzymatic activity of Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR):
3.5.1.98;

The structure of Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR), PDB code: 2vqw was solved by M.J.Bottomley, P.Lo Surdo, P.Di Giovine, A.Cirillo, R.Scarpelli, F.Ferrigno, P.Jones, P.Neddermann, R.De Francesco, C.Steinkuhler, P.Gallinari, A.Carfi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.0
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	137.911, 137.911, 69.519, 90.00, 90.00, 120.00
R / Rfree (%)	23.3 / 26.1

The structure of Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Potassium atom in the Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR) (pdb code 2vqw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR), PDB code: 2vqw:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR) within 5.0Å range: probe atom residue distance (Å) B Occ G:K1407 b:70.9 occ:1.00 O G:ASP196 2.6 68.5 1.0 O G:HIS198 2.6 65.2 1.0 OG G:SER217 2.9 73.7 1.0 OD1 G:ASP194 2.9 72.7 1.0 O G:ASP194 3.2 71.8 1.0 O G:LEU218 3.3 72.9 1.0 CG G:ASP194 3.5 72.5 1.0 C G:HIS198 3.7 65.2 1.0 C G:ASP194 3.7 71.5 1.0 C G:ASP196 3.7 68.5 1.0 C G:LEU218 3.7 72.8 1.0 N G:LEU218 3.8 73.5 1.0 N G:ASP196 3.8 69.7 1.0 CB G:HIS219 3.9 72.2 1.0 CB G:ASP194 4.1 71.9 1.0 CB G:SER217 4.1 74.0 1.0 OD2 G:ASP194 4.1 73.9 1.0 CA G:HIS199 4.2 64.5 1.0 N G:TRP195 4.2 71.0 1.0 CA G:ASP196 4.2 69.2 1.0 N G:HIS219 4.3 72.5 1.0 CA G:TRP195 4.3 70.5 1.0 C G:TRP195 4.3 70.2 1.0 CA G:HIS219 4.3 72.3 1.0 N G:HIS199 4.3 64.8 1.0 CB G:ASP196 4.4 69.3 1.0 N G:GLY200 4.4 64.9 1.0 CA G:LEU218 4.4 73.2 1.0 CA G:SER217 4.5 74.0 1.0 CA G:ASP194 4.5 71.8 1.0 ND1 G:HIS219 4.5 70.9 1.0 N G:HIS198 4.5 66.0 1.0 C G:SER217 4.5 73.9 1.0 C G:HIS199 4.7 64.8 1.0 CG G:HIS219 4.7 71.4 1.0 C G:VAL197 4.7 66.5 1.0 CA G:HIS198 4.7 65.4 1.0 OH G:TYR215 4.8 72.9 1.0 N G:VAL197 4.8 67.7 1.0

Potassium binding site 2 out of 2 in the Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Inhibitor-Free HDAC4 Catalytic Domain (with Gain-of-Function Mutation HIS332TYR) within 5.0Å range: probe atom residue distance (Å) B Occ G:K1408 b:74.8 occ:1.00 O G:PHE207 2.7 74.8 1.0 O G:ASP210 3.0 77.7 1.0 O G:VAL213 3.1 76.5 1.0 O G:PHE244 3.4 80.2 1.0 C G:PHE207 3.7 74.7 1.0 C G:PHE244 3.8 80.3 1.0 C G:ASP210 4.0 77.6 1.0 CB G:PHE207 4.0 74.1 1.0 CB G:PHE244 4.1 80.8 1.0 N G:ASP210 4.2 77.1 1.0 C G:VAL213 4.3 76.7 1.0 N G:ASN245 4.4 79.8 1.0 CA G:TYR208 4.4 75.8 1.0 N G:TYR208 4.5 75.2 1.0 O G:GLY241 4.5 83.8 1.0 CA G:PHE244 4.5 80.7 1.0 CB G:ASN245 4.5 79.2 1.0 C G:TYR208 4.5 76.2 1.0 CA G:PHE207 4.5 74.3 1.0 CA G:ASP210 4.6 77.4 1.0 N G:TYR215 4.6 75.4 1.0 CA G:ASN245 4.7 79.2 1.0 N G:SER209 4.7 76.4 1.0 CB G:ASP210 4.9 77.3 1.0 O G:TYR208 4.9 76.3 1.0 CA G:LEU214 4.9 76.2 1.0

M.J.Bottomley, P.Lo Surdo, P.Di Giovine, A.Cirillo, R.Scarpelli, F.Ferrigno, P.Jones, P.Neddermann, R.De Francesco, C.Steinkuhler, P.Gallinari, A.Carfi. Structural and Functional Analysis of the Human HDAC4 Catalytic Domain Reveals A Regulatory Structural Zinc-Binding Domain. J.Biol.Chem. V. 283 26694 2008.
ISSN: ISSN 0021-9258
PubMed: 18614528
DOI: 10.1074/JBC.M803514200