Potassium in PDB 6gg5: Crystal Structure of M2 Pyk in Complex with Tryptophan.

All present enzymatic activity of Crystal Structure of M2 Pyk in Complex with Tryptophan.:
2.7.1.40;

The structure of Crystal Structure of M2 Pyk in Complex with Tryptophan., PDB code: 6gg5 was solved by I.W.Mcnae, M.Yuan, M.D.Walkinshaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.54 / 3.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	96.880, 70.576, 168.502, 90.00, 106.02, 90.00
R / Rfree (%)	22.8 / 26.5

The binding sites of Potassium atom in the Crystal Structure of M2 Pyk in Complex with Tryptophan. (pdb code 6gg5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of M2 Pyk in Complex with Tryptophan., PDB code: 6gg5:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Crystal Structure of M2 Pyk in Complex with Tryptophan.


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 M2 Pyk in Complex with Tryptophan. within 5.0Å range: probe atom residue distance (Å) B Occ A:K605 b:45.5 occ:1.00 O A:THR114 2.9 48.5 1.0 OG A:SER77 2.9 54.1 1.0 OD1 A:ASN75 3.0 46.0 1.0 OD1 A:ASP113 3.1 45.8 1.0 OE2 A:GLU118 3.8 53.3 1.0 OG A:SER243 3.8 53.3 1.0 C A:THR114 4.0 49.2 1.0 CB A:SER77 4.0 53.9 1.0 CG A:ASN75 4.1 46.1 1.0 NZ A:LYS270 4.1 48.3 1.0 CG A:ASP113 4.1 46.0 1.0 O A:LYS115 4.2 50.8 1.0 O A:ASP113 4.3 46.6 1.0 CA A:LYS115 4.3 51.2 1.0 NH2 A:ARG73 4.4 41.0 1.0 N A:LYS115 4.5 50.7 1.0 ND2 A:ASN75 4.5 46.0 1.0 N A:SER77 4.6 52.2 1.0 C A:LYS115 4.6 51.3 1.0 C A:ASP113 4.7 46.7 1.0 OD2 A:ASP113 4.8 46.3 1.0 CB A:SER243 4.8 53.1 1.0 CA A:SER77 4.9 53.6 1.0 CB A:ASP113 4.9 45.9 1.0

Potassium binding site 2 out of 4 in the Crystal Structure of M2 Pyk in Complex with Tryptophan.


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 M2 Pyk in Complex with Tryptophan. within 5.0Å range: probe atom residue distance (Å) B Occ B:K605 b:61.4 occ:1.00 O B:THR114 2.7 51.1 1.0 OG B:SER77 3.0 57.8 1.0 OD1 B:ASP113 3.1 46.0 1.0 OD1 B:ASN75 3.1 51.9 1.0 OG B:SER243 3.7 50.0 1.0 C B:THR114 3.9 51.3 1.0 NZ B:LYS270 4.0 49.6 1.0 OE2 B:GLU118 4.0 65.6 1.0 CG B:ASP113 4.1 46.2 1.0 O B:LYS115 4.1 56.4 1.0 CB B:SER77 4.1 57.5 1.0 CG B:ASN75 4.2 52.2 1.0 CA B:LYS115 4.2 54.6 1.0 O B:ASP113 4.3 47.7 1.0 NH2 B:ARG73 4.4 48.2 1.0 N B:LYS115 4.5 53.2 1.0 C B:LYS115 4.5 55.5 1.0 N B:SER77 4.6 56.2 1.0 ND2 B:ASN75 4.7 52.9 1.0 C B:ASP113 4.7 47.7 1.0 CB B:SER243 4.7 50.2 1.0 OD2 B:ASP113 4.8 45.9 1.0 CA B:SER77 4.9 57.1 1.0 CB B:ASP113 4.9 46.6 1.0 N B:THR114 4.9 48.7 1.0

Potassium binding site 3 out of 4 in the Crystal Structure of M2 Pyk in Complex with Tryptophan.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of M2 Pyk in Complex with Tryptophan. within 5.0Å range: probe atom residue distance (Å) B Occ C:K603 b:66.7 occ:1.00 OG C:SER77 3.2 52.9 1.0 O C:THR114 3.2 48.9 1.0 OD1 C:ASP113 3.3 42.5 1.0 OD1 C:ASN75 3.3 45.0 1.0 NZ C:LYS270 3.9 48.9 1.0 OG C:SER243 3.9 53.6 1.0 CG C:ASN75 4.2 44.8 1.0 NH2 C:ARG73 4.3 38.5 1.0 CG C:ASP113 4.3 41.9 1.0 O C:LYS115 4.3 58.3 1.0 C C:THR114 4.3 49.5 1.0 CB C:SER77 4.3 52.4 1.0 CA C:LYS115 4.6 55.6 1.0 ND2 C:ASN75 4.6 45.2 1.0 O C:ASP113 4.6 43.1 1.0 C C:LYS115 4.8 57.8 1.0 OD2 C:ASP113 4.9 41.6 1.0 N C:LYS115 4.9 52.9 1.0 CB C:SER243 4.9 54.3 1.0 N C:SER77 5.0 50.4 1.0

Potassium binding site 4 out of 4 in the Crystal Structure of M2 Pyk in Complex with Tryptophan.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of M2 Pyk in Complex with Tryptophan. within 5.0Å range: probe atom residue distance (Å) B Occ D:K603 b:79.0 occ:1.00 O D:THR114 2.8 59.9 1.0 OD1 D:ASP113 2.8 54.1 1.0 OD1 D:ASN75 2.9 49.8 1.0 OG D:SER77 3.1 60.5 1.0 CG D:ASP113 3.8 53.5 1.0 OG D:SER243 3.8 45.7 1.0 C D:THR114 3.9 60.4 1.0 CG D:ASN75 4.0 49.6 1.0 NZ D:LYS270 4.0 43.6 1.0 O D:ASP113 4.0 56.9 1.0 CB D:SER77 4.2 59.4 1.0 NH2 D:ARG73 4.2 45.0 1.0 CA D:LYS115 4.4 64.7 1.0 O D:LYS115 4.4 65.0 1.0 C D:ASP113 4.5 55.8 1.0 N D:LYS115 4.5 62.8 1.0 ND2 D:ASN75 4.5 49.6 1.0 N D:SER77 4.6 56.6 1.0 OD2 D:ASP113 4.6 53.4 1.0 CB D:ASP113 4.6 53.6 1.0 C D:LYS115 4.8 65.6 1.0 N D:THR114 4.8 57.4 1.0 CA D:SER77 4.9 59.0 1.0 CB D:SER243 4.9 46.0 1.0 CA D:THR114 5.0 59.0 1.0

M.Yuan, I.W.Mcnae, Y.Chen, E.A.Blackburn, M.A.Wear, P.A.M.Michels, L.A.Fothergill-Gilmore, T.Hupp, M.D.Walkinshaw. An Allostatic Mechanism For M2 Pyruvate Kinase As An Amino-Acid Sensor. Biochem. J. V. 475 1821 2018.
ISSN: ESSN 1470-8728
PubMed: 29748232
DOI: 10.1042/BCJ20180171