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Potassium in PDB 1pl0: Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC

Enzymatic activity of Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC

All present enzymatic activity of Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC:
2.1.2.3; 3.5.4.10;

Protein crystallography data

The structure of Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC, PDB code: 1pl0 was solved by C.G.Cheong, S.E.Greasley, P.A.Horton, G.P.Beardsley, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.120, 92.970, 178.490, 90.00, 91.19, 90.00
R / Rfree (%) 21.3 / 27.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC (pdb code 1pl0). 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 Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC, PDB code: 1pl0:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 1pl0

Go back to Potassium Binding Sites List in 1pl0
Potassium binding site 1 out of 4 in the Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC


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 Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1001

b:16.1
occ:1.00
 O A:THR428 2.6 10.2 1.0
O A:VAL425 2.6 5.9 1.0
O A:LEU589 2.7 9.7 1.0
OD1 A:ASP539 2.8 23.2 1.0
OG A:SER432 2.9 16.9 1.0
OG A:SER430 3.4 17.5 1.0
N A:HIS591 3.6 14.2 1.0
CG A:ASP539 3.7 21.1 1.0
C A:THR428 3.7 9.2 1.0
CB A:HIS591 3.7 17.4 1.0
CB A:ASP539 3.7 18.2 1.0
C A:VAL425 3.8 7.3 1.0
C A:LEU589 3.9 10.1 1.0
C A:PHE590 4.1 12.3 1.0
N A:THR428 4.1 9.5 1.0
CA A:PHE590 4.2 10.3 1.0
CB A:SER432 4.3 14.6 1.0
CA A:HIS591 4.3 15.9 1.0
N A:SER430 4.3 14.8 1.0
CG2 A:VAL425 4.3 10.3 1.0
CA A:THR428 4.4 8.8 1.0
O A:LYS426 4.4 8.5 1.0
CB A:SER430 4.4 16.2 1.0
CB A:THR428 4.4 5.8 1.0
C A:GLN429 4.4 12.7 1.0
CA A:SER430 4.4 16.8 1.0
C A:LYS426 4.5 9.6 1.0
N A:PHE590 4.5 9.2 1.0
CA A:LYS426 4.6 8.4 1.0
N A:LYS426 4.6 7.5 1.0
O A:GLN429 4.6 12.7 1.0
CA A:VAL425 4.7 7.8 1.0
CB A:LEU589 4.8 7.7 1.0
N A:GLN429 4.8 10.6 1.0
O A:HIS591 4.8 17.0 1.0
OD2 A:ASP539 4.9 25.0 1.0
CA A:GLN429 5.0 11.4 1.0
CA A:LEU589 5.0 10.1 1.0

Potassium binding site 2 out of 4 in 1pl0

Go back to Potassium Binding Sites List in 1pl0
Potassium binding site 2 out of 4 in the Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC


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 Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1002

b:12.3
occ:1.00
 O B:VAL425 2.6 8.0 1.0
O B:LEU589 2.6 9.9 1.0
O B:THR428 2.6 12.4 1.0
OG B:SER432 3.0 16.2 1.0
OD1 B:ASP539 3.1 13.1 1.0
OG B:SER430 3.2 13.4 1.0
CB B:HIS591 3.6 14.8 1.0
N B:HIS591 3.6 12.8 1.0
CB B:ASP539 3.7 16.0 1.0
C B:THR428 3.7 11.3 1.0
C B:LEU589 3.8 10.0 1.0
C B:VAL425 3.8 10.4 1.0
CG B:ASP539 3.8 18.6 1.0
C B:PHE590 3.9 11.8 1.0
CA B:PHE590 4.0 9.2 1.0
O B:LYS426 4.1 9.3 1.0
CA B:HIS591 4.2 14.3 1.0
N B:THR428 4.2 7.6 1.0
CB B:SER432 4.2 15.1 1.0
C B:LYS426 4.3 7.9 1.0
CB B:SER430 4.3 13.6 1.0
N B:SER430 4.4 12.9 1.0
CA B:THR428 4.4 7.8 1.0
N B:PHE590 4.4 9.8 1.0
CA B:LYS426 4.5 9.1 1.0
CB B:THR428 4.5 8.5 1.0
C B:GLN429 4.5 13.0 1.0
CA B:SER430 4.6 13.5 1.0
N B:LYS426 4.6 10.1 1.0
O B:PHE590 4.6 10.6 1.0
CB B:LEU589 4.8 10.9 1.0
O B:HIS591 4.8 17.0 1.0
N B:GLN429 4.8 11.9 1.0
CG B:HIS591 4.8 15.7 1.0
CA B:VAL425 4.8 11.3 1.0
CG2 B:VAL425 4.9 13.9 1.0
O B:GLN429 4.9 9.2 1.0
CA B:LEU589 4.9 10.2 1.0
CA B:GLN429 5.0 12.0 1.0

Potassium binding site 3 out of 4 in 1pl0

Go back to Potassium Binding Sites List in 1pl0
Potassium binding site 3 out of 4 in the Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC


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 Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1003

b:17.7
occ:1.00
 O C:LEU589 2.4 14.8 1.0
O C:VAL425 2.6 13.2 1.0
O C:THR428 2.7 15.7 1.0
OG C:SER432 3.0 23.6 1.0
OD1 C:ASP539 3.1 20.7 1.0
OG C:SER430 3.4 13.8 1.0
N C:HIS591 3.5 16.1 1.0
CB C:ASP539 3.6 17.8 1.0
C C:LEU589 3.6 12.8 1.0
CB C:HIS591 3.7 15.4 1.0
C C:VAL425 3.8 13.5 1.0
CG C:ASP539 3.8 21.3 1.0
C C:THR428 3.8 11.9 1.0
C C:PHE590 4.0 15.8 1.0
CA C:PHE590 4.0 13.5 1.0
CG1 C:VAL425 4.1 16.1 1.0
N C:THR428 4.2 9.1 1.0
CA C:HIS591 4.2 16.8 1.0
CB C:SER432 4.2 19.5 1.0
N C:PHE590 4.3 12.7 1.0
C C:LYS426 4.4 10.2 1.0
CA C:THR428 4.4 10.2 1.0
O C:LYS426 4.5 10.7 1.0
N C:SER430 4.5 13.6 1.0
CB C:THR428 4.5 10.1 1.0
CA C:LYS426 4.5 11.2 1.0
CB C:LEU589 4.6 12.7 1.0
CB C:SER430 4.6 14.9 1.0
N C:LYS426 4.6 11.7 1.0
C C:GLN429 4.7 12.9 1.0
CA C:SER430 4.7 16.4 1.0
CA C:VAL425 4.7 14.2 1.0
CA C:LEU589 4.8 11.1 1.0
O C:PHE590 4.8 19.3 1.0
N C:GLN429 4.9 12.0 1.0
N C:TYR427 4.9 8.5 1.0
O C:GLN429 4.9 13.1 1.0
O C:HIS591 5.0 18.4 1.0

Potassium binding site 4 out of 4 in 1pl0

Go back to Potassium Binding Sites List in 1pl0
Potassium binding site 4 out of 4 in the Crystal Structure of Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC


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 Human Atic in Complex with Folate- Based Inhibitor, BW2315U89UC within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K1004

b:17.6
occ:1.00
 O D:THR428 2.7 16.3 1.0
O D:VAL425 2.7 16.8 1.0
OD1 D:ASP539 2.8 15.5 1.0
OG D:SER432 2.8 26.1 1.0
O D:LEU589 2.9 11.9 1.0
OG D:SER430 3.0 17.4 1.0
N D:HIS591 3.5 14.3 1.0
CG D:ASP539 3.6 18.7 1.0
CB D:ASP539 3.7 18.4 1.0
CB D:HIS591 3.7 16.5 1.0
C D:THR428 3.7 14.1 1.0
C D:VAL425 3.8 15.1 1.0
C D:LEU589 3.9 12.2 1.0
C D:PHE590 4.0 12.9 1.0
CB D:SER432 4.0 21.7 1.0
CA D:PHE590 4.0 11.5 1.0
N D:SER430 4.1 16.8 1.0
CB D:SER430 4.2 15.8 1.0
CA D:HIS591 4.2 15.7 1.0
CA D:SER430 4.3 18.2 1.0
N D:THR428 4.3 11.7 1.0
C D:GLN429 4.3 16.7 1.0
CB D:THR428 4.3 13.2 1.0
CA D:THR428 4.4 13.0 1.0
N D:PHE590 4.4 11.7 1.0
O D:LYS426 4.6 14.5 1.0
CA D:VAL425 4.6 14.7 1.0
C D:LYS426 4.7 12.8 1.0
N D:GLN429 4.7 15.7 1.0
O D:GLN429 4.7 14.9 1.0
N D:LYS426 4.7 13.7 1.0
CA D:LYS426 4.7 12.3 1.0
CB D:VAL425 4.8 15.7 1.0
CA D:GLN429 4.8 16.8 1.0
O D:HIS591 4.8 18.4 1.0
N D:SER432 4.8 20.8 1.0
OD2 D:ASP539 4.8 17.4 1.0
O D:PHE590 4.9 12.5 1.0
CG D:HIS591 5.0 15.9 1.0
CA D:SER432 5.0 21.6 1.0

Reference:

C.G.Cheong, D.W.Wolan, S.E.Greasley, P.A.Horton, G.P.Beardsley, I.A.Wilson. Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-Carboxamide Ribonucleotide Transformylase/Imp Cyclohydrolase in Complex with Potent Sulfonyl-Containing Antifolates. J.Biol.Chem. V. 279 18034 2004.
ISSN: ISSN 0021-9258
PubMed: 14966129
DOI: 10.1074/JBC.M313691200
Page generated: Mon Aug 12 05:12:23 2024

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