Potassium in PDB 2vgi: Human Erythrocyte Pyruvate Kinase: R486W Mutant

All present enzymatic activity of Human Erythrocyte Pyruvate Kinase: R486W Mutant:
2.7.1.40;

The structure of Human Erythrocyte Pyruvate Kinase: R486W Mutant, PDB code: 2vgi was solved by G.Valentini, L.Chiarelli, R.Fortin, M.Dolzan, A.Galizzi, D.J.Abraham, C.Wang, P.Bianchi, A.Zanella, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.87
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.705, 171.164, 85.050, 90.00, 91.61, 90.00
R / Rfree (%)	25.7 / 31.1

The structure of Human Erythrocyte Pyruvate Kinase: R486W Mutant also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Potassium atom in the Human Erythrocyte Pyruvate Kinase: R486W Mutant (pdb code 2vgi). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Human Erythrocyte Pyruvate Kinase: R486W Mutant, PDB code: 2vgi:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Human Erythrocyte Pyruvate Kinase: R486W Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Erythrocyte Pyruvate Kinase: R486W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K1576 b:2.0 occ:1.00 OD1 A:ASP156 2.8 2.0 1.0 O A:THR157 2.8 2.0 1.0 OG A:SER120 3.1 2.0 1.0 OG A:SER286 3.2 2.0 1.0 O2P A:PGA1575 3.2 2.0 1.0 OD1 A:ASN118 3.4 2.0 1.0 NZ A:LYS313 3.5 2.0 1.0 CA A:LYS158 3.8 2.0 1.0 O A:ASP156 3.9 2.0 1.0 C A:THR157 3.9 2.0 1.0 CG A:ASP156 3.9 2.0 1.0 CB A:SER120 4.0 2.0 1.0 OE2 A:GLU161 4.0 2.0 1.0 O A:LYS158 4.1 2.0 1.0 C A:LYS158 4.3 2.0 1.0 N A:LYS158 4.4 2.0 1.0 P A:PGA1575 4.4 2.0 1.0 CG A:ASN118 4.4 2.0 1.0 CB A:SER286 4.4 2.0 1.0 N A:SER120 4.5 2.0 1.0 O4P A:PGA1575 4.5 2.0 1.0 OD2 A:ASP156 4.5 2.0 1.0 C A:ASP156 4.5 2.0 1.0 CA A:SER120 4.7 2.0 1.0 CB A:LYS158 4.8 2.0 1.0 NH2 A:ARG116 4.8 2.0 1.0 O1P A:PGA1575 4.8 2.0 1.0 CE A:LYS313 4.8 2.0 1.0 CB A:ASP156 4.9 2.0 1.0 ND2 A:ASN118 5.0 2.0 1.0 CD A:GLU161 5.0 2.0 1.0

Potassium binding site 2 out of 4 in the Human Erythrocyte Pyruvate Kinase: R486W Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human Erythrocyte Pyruvate Kinase: R486W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:K1576 b:2.0 occ:1.00 OD1 B:ASP156 2.8 2.0 1.0 OD1 B:ASN118 2.8 2.0 1.0 O B:THR157 3.2 2.0 1.0 O2P B:PGA1575 3.2 2.0 1.0 OG B:SER120 3.2 2.0 1.0 OG B:SER286 3.6 2.0 1.0 CG B:ASP156 3.7 2.0 1.0 CG B:ASN118 3.8 2.0 1.0 CB B:SER120 3.8 2.0 1.0 O B:ASP156 3.9 2.0 1.0 NZ B:LYS313 3.9 2.0 1.0 CA B:LYS158 4.0 2.0 1.0 C B:THR157 4.1 2.0 1.0 O B:LYS158 4.2 2.0 1.0 OD2 B:ASP156 4.3 2.0 1.0 N B:SER120 4.3 2.0 1.0 ND2 B:ASN118 4.3 2.0 1.0 P B:PGA1575 4.4 2.0 1.0 NH2 B:ARG116 4.4 2.0 1.0 N B:LYS158 4.5 2.0 1.0 O4P B:PGA1575 4.5 2.0 1.0 C B:ASP156 4.5 2.0 1.0 C B:LYS158 4.5 2.0 1.0 CA B:SER120 4.5 2.0 1.0 CB B:ASP156 4.6 2.0 1.0 OE2 B:GLU161 4.7 2.0 1.0 CB B:SER286 4.8 2.0 1.0 O1P B:PGA1575 5.0 2.0 1.0 N B:PHE119 5.0 2.0 1.0 CB B:ASN118 5.0 2.0 1.0

Potassium binding site 3 out of 4 in the Human Erythrocyte Pyruvate Kinase: R486W Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Human Erythrocyte Pyruvate Kinase: R486W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:K1576 b:2.0 occ:1.00 OD1 C:ASN118 2.4 2.0 1.0 OD1 C:ASP156 2.9 2.0 1.0 O2P C:PGA1575 2.9 2.0 1.0 OG C:SER120 3.0 2.0 1.0 CG C:ASN118 3.5 2.0 1.0 CB C:SER120 3.5 2.0 1.0 O C:THR157 3.6 2.0 1.0 CG C:ASP156 3.8 2.0 1.0 ND2 C:ASN118 4.0 2.0 1.0 N C:SER120 4.0 2.0 1.0 NZ C:LYS313 4.1 2.0 1.0 P C:PGA1575 4.1 2.0 1.0 OE2 C:GLU161 4.2 2.0 1.0 CA C:LYS158 4.2 2.0 1.0 O C:ASP156 4.2 2.0 1.0 OG C:SER286 4.2 2.0 1.0 NH2 C:ARG116 4.2 2.0 1.0 CA C:SER120 4.3 2.0 1.0 C C:THR157 4.4 2.0 1.0 O4P C:PGA1575 4.4 2.0 1.0 O C:LYS158 4.4 2.0 1.0 OD2 C:ASP156 4.6 2.0 1.0 CB C:ASP156 4.6 2.0 1.0 N C:LYS158 4.6 2.0 1.0 CB C:ASN118 4.7 2.0 1.0 N C:PHE119 4.7 2.0 1.0 C C:ASP156 4.7 2.0 1.0 C C:LYS158 4.8 2.0 1.0 O1P C:PGA1575 4.8 2.0 1.0 CA C:ASN118 4.8 2.0 1.0 CD C:GLU161 4.9 2.0 1.0 C C:ASN118 4.9 2.0 1.0

Potassium binding site 4 out of 4 in the Human Erythrocyte Pyruvate Kinase: R486W Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Human Erythrocyte Pyruvate Kinase: R486W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:K1576 b:2.0 occ:1.00 OD1 D:ASP156 2.5 2.0 1.0 OG D:SER120 2.8 2.0 1.0 O D:THR157 2.9 2.0 1.0 OD1 D:ASN118 3.0 2.0 1.0 OG D:SER286 3.7 2.0 1.0 CG D:ASP156 3.7 2.0 1.0 CA D:LYS158 3.7 2.0 1.0 O2P D:PGA1575 3.7 2.0 1.0 CB D:SER120 3.8 2.0 1.0 O D:ASP156 3.8 2.0 1.0 C D:THR157 3.8 2.0 1.0 CG D:ASN118 4.0 2.0 1.0 NZ D:LYS313 4.0 2.0 1.0 N D:SER120 4.0 2.0 1.0 O D:LYS158 4.1 2.0 1.0 N D:LYS158 4.2 2.0 1.0 OE2 D:GLU161 4.2 2.0 1.0 C D:LYS158 4.3 2.0 1.0 CA D:SER120 4.4 2.0 1.0 C D:ASP156 4.4 2.0 1.0 OD2 D:ASP156 4.4 2.0 1.0 ND2 D:ASN118 4.4 2.0 1.0 CB D:ASP156 4.7 2.0 1.0 NH2 D:ARG116 4.7 2.0 1.0 CB D:LYS158 4.7 2.0 1.0 N D:PHE119 4.7 2.0 1.0 CB D:SER286 4.8 2.0 1.0 N D:THR157 4.9 2.0 1.0 P D:PGA1575 4.9 2.0 1.0 C D:PHE119 4.9 2.0 1.0

G.Valentini, L.R.Chiarelli, R.Fortin, M.Dolzan, A.Galizzi, D.J.Abraham, C.Wang, P.Bianchi, A.Zanella, A.Mattevi. Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia. J.Biol.Chem. V. 277 23807 2002.
ISSN: ISSN 0021-9258
PubMed: 11960989
DOI: 10.1074/JBC.M202107200