Potassium in PDB 3act: Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant

All present enzymatic activity of Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant:
2.4.1.20;

The structure of Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant, PDB code: 3act was solved by M.Hidaka, M.A.Hayashi, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	84.360, 98.315, 104.332, 90.00, 102.72, 90.00
R / Rfree (%)	12.8 / 17.6

The binding sites of Potassium atom in the Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant (pdb code 3act). 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 Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant, PDB code: 3act:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant


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 Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K2903 b:21.2 occ:1.00 O A:TRP488 2.6 8.2 1.0 O A:HOH1474 2.7 19.9 1.0 O A:HOH1105 2.8 9.6 1.0 O A:HOH1152 2.8 26.1 1.0 OD1 A:ASP490 3.2 13.4 1.0 O A:HOH1273 3.2 20.4 1.0 NH1 A:ARG367 3.4 9.0 1.0 CG A:ASP490 3.6 12.6 1.0 C A:TRP488 3.8 9.6 1.0 OD2 A:ASP490 4.0 10.4 1.0 CE2 A:TRP488 4.0 11.9 1.0 NE1 A:TRP488 4.0 10.8 1.0 N A:ASP490 4.1 9.7 1.0 CZ A:ARG367 4.1 10.5 1.0 O4 A:PO42902 4.2 12.0 1.0 CD2 A:TRP488 4.3 12.1 1.0 O4 A:BGC2901 4.3 10.5 1.0 CD1 A:TRP488 4.3 7.1 1.0 CZ2 A:TRP488 4.3 12.1 1.0 CB A:ASP490 4.4 9.2 1.0 CD A:ARG367 4.5 11.4 1.0 O A:HOH1499 4.5 31.7 1.0 CG A:TRP488 4.5 5.8 1.0 NE A:ARG367 4.6 10.9 1.0 CA A:ASN489 4.7 9.6 1.0 O3 A:PO42902 4.7 7.4 1.0 N A:ASN489 4.7 8.9 1.0 CA A:TRP488 4.7 7.3 1.0 CA A:ASP490 4.8 9.8 1.0 OE2 A:GLU659 4.9 9.8 1.0 C A:ASN489 4.9 11.1 1.0 NH2 A:ARG367 4.9 8.7 1.0 CE3 A:TRP488 4.9 10.9 1.0 CH2 A:TRP488 4.9 11.9 1.0 CE2 A:PHE664 5.0 9.2 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant


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 Cellvibrio Gilvus Cellobiose Phosphorylase Histidine Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:K3903 b:22.6 occ:1.00 O B:TRP488 2.6 7.3 1.0 O B:HOH823 2.7 17.8 1.0 O B:HOH1398 2.7 15.3 1.0 O B:HOH1525 2.7 18.6 1.0 OD1 B:ASP490 3.2 14.4 1.0 NH1 B:ARG367 3.3 10.4 1.0 O B:HOH930 3.3 24.8 1.0 CG B:ASP490 3.6 14.4 1.0 C B:TRP488 3.8 9.1 1.0 OD2 B:ASP490 3.9 14.6 1.0 NE1 B:TRP488 4.0 9.8 1.0 CE2 B:TRP488 4.0 12.1 1.0 O1 B:PO43902 4.1 12.4 1.0 CZ B:ARG367 4.1 11.6 1.0 N B:ASP490 4.2 9.1 1.0 O4 B:BGC3901 4.3 10.7 1.0 CD1 B:TRP488 4.3 10.0 1.0 CD2 B:TRP488 4.3 12.2 1.0 CB B:ASP490 4.4 10.0 1.0 CD B:ARG367 4.4 9.2 1.0 CZ2 B:TRP488 4.4 12.8 1.0 O B:HOH1062 4.4 26.4 1.0 CG B:TRP488 4.5 8.2 1.0 NE B:ARG367 4.5 10.5 1.0 CA B:ASN489 4.7 7.9 1.0 O2 B:PO43902 4.7 9.1 1.0 CA B:TRP488 4.7 9.0 1.0 N B:ASN489 4.7 8.2 1.0 CA B:ASP490 4.9 9.8 1.0 C B:ASN489 4.9 9.5 1.0 NH2 B:ARG367 4.9 11.0 1.0 OE2 B:GLU659 4.9 10.0 1.0 CE3 B:TRP488 4.9 12.3 1.0 CH2 B:TRP488 5.0 12.6 1.0

T.Arai, M.A.Hayashi, M.Hidaka, M.Kitaoka, T.Wakagi, H.Shoun, S.Fushinobu. Engineering of Cellobiose Phosphorylase To Be Published.