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Potassium in PDB 5x0i: Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine

Enzymatic activity of Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine

All present enzymatic activity of Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine:
2.7.1.40;

Protein crystallography data

The structure of Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine, PDB code: 5x0i was solved by W.C.Wang, T.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.64
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 116.601, 137.875, 149.709, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 21.8

Other elements in 5x0i:

The structure of Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine (pdb code 5x0i). 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 PKM2 R399E Mutant Complexed with Fbp and Serine, PDB code: 5x0i:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 5x0i

Go back to Potassium Binding Sites List in 5x0i
Potassium binding site 1 out of 4 in the Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine


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 PKM2 R399E Mutant Complexed with Fbp and Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K605

b:44.5
occ:1.00
 O A:THR114 2.6 39.0 1.0
OD1 A:ASN75 2.7 29.9 1.0
OG A:SER77 2.8 39.0 1.0
OD1 A:ASP113 2.9 42.1 1.0
C A:THR114 3.5 33.9 1.0
CG A:ASP113 3.7 37.8 1.0
OG A:SER243 3.7 21.5 1.0
CG A:ASN75 3.8 31.5 1.0
NZ A:LYS270 3.9 26.3 1.0
CB A:SER77 4.0 37.5 1.0
CA A:LYS115 4.1 34.1 1.0
O A:ASP113 4.1 30.6 1.0
N A:LYS115 4.1 34.6 1.0
ND2 A:ASN75 4.2 27.7 1.0
N A:SER77 4.2 35.1 1.0
OD2 A:ASP113 4.3 32.4 1.0
O A:LYS115 4.3 31.9 1.0
C A:ASP113 4.3 30.7 1.0
OE2 A:GLU118 4.4 44.5 1.0
CB A:ASP113 4.4 35.9 1.0
N A:THR114 4.6 30.2 1.0
C A:LYS115 4.6 31.1 1.0
CA A:SER77 4.6 36.5 1.0
CA A:THR114 4.6 31.9 1.0
NH2 A:ARG73 4.7 33.2 1.0
N A:PHE76 4.8 29.4 1.0
CB A:SER243 4.8 23.3 1.0
CA A:ASP113 5.0 33.0 1.0

Potassium binding site 2 out of 4 in 5x0i

Go back to Potassium Binding Sites List in 5x0i
Potassium binding site 2 out of 4 in the Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine


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 PKM2 R399E Mutant Complexed with Fbp and Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K605

b:42.2
occ:1.00
 O B:HOH703 2.5 31.9 1.0
OD1 B:ASP113 2.6 41.2 1.0
OD1 B:ASN75 2.7 33.9 1.0
O B:THR114 2.9 28.8 1.0
OG B:SER77 3.0 34.5 1.0
CG B:ASN75 3.6 29.9 1.0
OG B:SER243 3.7 26.6 1.0
CG B:ASP113 3.8 33.1 1.0
C B:THR114 3.8 30.1 1.0
O B:ASP113 3.9 31.2 1.0
CB B:SER77 3.9 35.8 1.0
ND2 B:ASN75 4.0 30.3 1.0
NZ B:LYS270 4.0 35.1 1.0
N B:SER77 4.2 35.2 1.0
CA B:LYS115 4.2 30.6 1.0
OE2 B:GLU118 4.2 47.4 1.0
N B:LYS115 4.3 31.9 1.0
NH2 B:ARG73 4.3 34.1 1.0
C B:ASP113 4.4 30.2 1.0
OD2 B:ASP113 4.4 32.2 1.0
O B:LYS115 4.4 38.5 1.0
CA B:SER77 4.5 33.4 1.0
C B:LYS115 4.7 32.0 1.0
CB B:ASP113 4.7 31.6 1.0
N B:THR114 4.7 30.8 1.0
CB B:SER243 4.8 28.2 1.0
CA B:THR114 4.9 29.9 1.0
N B:PHE76 4.9 30.8 1.0
CB B:ASN75 5.0 26.8 1.0

Potassium binding site 3 out of 4 in 5x0i

Go back to Potassium Binding Sites List in 5x0i
Potassium binding site 3 out of 4 in the Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine


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 PKM2 R399E Mutant Complexed with Fbp and Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K605

b:44.8
occ:1.00
 OD1 C:ASP113 2.6 46.7 1.0
O C:THR114 2.8 31.9 1.0
OD1 C:ASN75 2.9 42.2 1.0
OG C:SER77 2.9 42.2 1.0
CG C:ASP113 3.6 39.2 1.0
C C:THR114 3.7 31.1 1.0
OG C:SER243 3.7 30.5 1.0
O C:ASP113 3.7 37.0 1.0
CB C:SER77 3.9 46.9 1.0
CG C:ASN75 3.9 35.3 1.0
NZ C:LYS270 4.0 35.7 1.0
CA C:LYS115 4.1 31.3 1.0
C C:ASP113 4.1 33.9 1.0
O C:LYS115 4.2 36.2 1.0
OD2 C:ASP113 4.2 40.5 1.0
OE2 C:GLU118 4.2 48.4 1.0
N C:LYS115 4.2 31.8 1.0
NH2 C:ARG73 4.2 35.5 1.0
N C:SER77 4.3 43.2 1.0
CB C:ASP113 4.4 32.3 1.0
ND2 C:ASN75 4.5 35.0 1.0
N C:THR114 4.5 33.2 1.0
C C:LYS115 4.6 32.5 1.0
CA C:SER77 4.6 44.3 1.0
CA C:THR114 4.7 30.6 1.0
CB C:SER243 4.8 30.8 1.0
N C:PHE76 4.9 37.6 1.0
CA C:ASP113 4.9 32.7 1.0

Potassium binding site 4 out of 4 in 5x0i

Go back to Potassium Binding Sites List in 5x0i
Potassium binding site 4 out of 4 in the Crystal Structure of PKM2 R399E Mutant Complexed with Fbp and Serine


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 PKM2 R399E Mutant Complexed with Fbp and Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K605

b:52.7
occ:1.00
 OD1 D:ASN75 2.7 37.3 1.0
OG D:SER77 2.7 47.6 1.0
OD1 D:ASP113 2.7 43.6 1.0
O D:THR114 2.9 51.4 1.0
OG D:SER243 3.7 31.0 1.0
CG D:ASP113 3.7 45.4 1.0
C D:THR114 3.8 44.2 1.0
CG D:ASN75 3.8 37.4 1.0
OE2 D:GLU118 3.9 42.5 1.0
CB D:SER77 3.9 45.5 1.0
NZ D:LYS270 4.1 38.2 1.0
O D:ASP113 4.1 40.1 1.0
CA D:LYS115 4.2 46.6 1.0
N D:LYS115 4.3 49.7 1.0
ND2 D:ASN75 4.3 36.7 1.0
N D:SER77 4.3 50.6 1.0
C D:ASP113 4.4 38.9 1.0
OD2 D:ASP113 4.4 40.7 1.0
O D:LYS115 4.4 47.1 1.0
CB D:ASP113 4.5 41.4 1.0
CA D:SER77 4.7 51.7 1.0
C D:LYS115 4.7 43.2 1.0
N D:THR114 4.7 35.8 1.0
NH2 D:ARG73 4.8 37.4 1.0
CB D:SER243 4.8 33.6 1.0
CA D:THR114 4.9 37.5 1.0
N D:PHE76 4.9 42.6 1.0
MG D:MG604 4.9 46.1 1.0
O3 D:PYR603 4.9 45.7 1.0

Reference:

T.J.Chen, H.J.Wang, J.S.Liu, H.H.Cheng, S.C.Hsu, M.C.Wu, C.H.Lu, Y.F.Wu, J.W.Wu, Y.Y.Liu, H.J.Kung, W.C.Wang. Mutations in the PKM2 Exon-10 Region Are Associated with Reduced Allostery and Increased Nuclear Translocation. Commun Biol V. 2 105 2019.
ISSN: ESSN 2399-3642
PubMed: 30911680
DOI: 10.1038/S42003-019-0343-4
Page generated: Mon Aug 12 15:01:22 2024

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