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Potassium in PDB 1pkx: Crystal Structure of Human Atic in Complex with Xmp

Enzymatic activity of Crystal Structure of Human Atic in Complex with Xmp

All present enzymatic activity of Crystal Structure of Human Atic in Complex with Xmp:
2.1.2.3; 3.5.4.10;

Protein crystallography data

The structure of Crystal Structure of Human Atic in Complex with Xmp, PDB code: 1pkx was solved by D.W.Wolan, C.G.Cheong, S.E.Greasley, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.520, 93.560, 179.880, 90.00, 91.09, 90.00
R / Rfree (%) 21.1 / 24.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human Atic in Complex with Xmp (pdb code 1pkx). 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 Xmp, PDB code: 1pkx:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 1pkx

Go back to Potassium Binding Sites List in 1pkx
Potassium binding site 1 out of 4 in the Crystal Structure of Human Atic in Complex with Xmp


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 Xmp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2001

b:16.0
occ:1.00
 O A:VAL425 2.6 16.8 1.0
O A:THR428 2.6 15.8 1.0
O A:LEU589 2.8 17.2 1.0
OD1 A:ASP539 2.9 21.5 1.0
OG A:SER432 3.0 22.4 1.0
OG A:SER430 3.1 17.5 1.0
CB A:HIS591 3.7 16.5 1.0
C A:THR428 3.7 17.1 1.0
C A:VAL425 3.8 18.3 1.0
CB A:SER432 3.8 21.0 1.0
CG A:ASP539 3.8 19.6 1.0
N A:HIS591 3.8 15.7 1.0
CB A:ASP539 3.9 19.6 1.0
C A:LEU589 4.0 18.0 1.0
C A:PHE590 4.2 18.1 1.0
N A:THR428 4.2 12.0 1.0
N A:SER430 4.2 13.4 1.0
CB A:SER430 4.2 14.9 1.0
CA A:PHE590 4.3 17.2 1.0
CA A:SER430 4.3 15.0 1.0
CA A:THR428 4.4 14.4 1.0
CA A:HIS591 4.4 16.2 1.0
C A:GLN429 4.4 17.4 1.0
CB A:THR428 4.5 14.5 1.0
O A:LYS426 4.6 15.3 1.0
CA A:VAL425 4.6 18.2 1.0
C A:LYS426 4.6 16.8 1.0
N A:PHE590 4.6 17.9 1.0
N A:LYS426 4.7 17.1 1.0
O A:HOH2099 4.7 24.8 1.0
CA A:LYS426 4.7 17.0 1.0
N A:GLN429 4.7 17.4 1.0
CB A:VAL425 4.8 21.0 1.0
O A:GLN429 4.8 14.6 1.0
O A:HIS591 4.8 16.6 1.0
N A:SER432 4.8 19.2 1.0
CG A:HIS591 4.8 16.8 1.0
O A:PHE590 4.9 17.2 1.0
CA A:GLN429 4.9 17.7 1.0
CA A:SER432 4.9 20.5 1.0
CB A:LEU589 5.0 17.6 1.0
OD2 A:ASP539 5.0 21.8 1.0

Potassium binding site 2 out of 4 in 1pkx

Go back to Potassium Binding Sites List in 1pkx
Potassium binding site 2 out of 4 in the Crystal Structure of Human Atic in Complex with Xmp


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 Xmp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K2002

b:18.0
occ:1.00
 O B:VAL425 2.7 16.2 1.0
O B:LEU589 2.7 15.8 1.0
O B:THR428 2.7 16.2 1.0
OD1 B:ASP539 2.7 18.6 1.0
OG B:SER432 2.9 24.2 1.0
OG B:SER430 3.0 19.4 1.0
CG B:ASP539 3.7 22.8 1.0
CB B:HIS591 3.7 17.9 1.0
N B:HIS591 3.8 17.0 1.0
CB B:ASP539 3.8 22.7 1.0
CB B:SER432 3.8 20.4 1.0
C B:VAL425 3.8 17.3 1.0
C B:LEU589 3.8 16.7 1.0
C B:THR428 3.9 16.5 1.0
C B:PHE590 4.1 18.0 1.0
CA B:PHE590 4.1 14.8 1.0
CB B:SER430 4.2 17.9 1.0
N B:SER430 4.3 17.3 1.0
N B:THR428 4.3 15.1 1.0
CA B:SER430 4.4 18.7 1.0
CA B:HIS591 4.4 17.7 1.0
O B:HOH2189 4.4 37.5 1.0
N B:PHE590 4.5 15.6 1.0
CG1 B:VAL425 4.5 24.1 1.0
CB B:THR428 4.5 15.6 1.0
CA B:THR428 4.5 16.0 1.0
C B:GLN429 4.6 17.1 1.0
C B:LYS426 4.6 15.8 1.0
O B:LYS426 4.6 15.1 1.0
CA B:LYS426 4.7 16.2 1.0
CA B:VAL425 4.7 17.9 1.0
N B:LYS426 4.7 16.4 1.0
N B:SER432 4.8 21.0 1.0
O B:PHE590 4.8 14.9 1.0
OD2 B:ASP539 4.9 21.1 1.0
CB B:LEU589 4.9 16.8 1.0
O B:HIS591 4.9 16.5 1.0
CG B:HIS591 4.9 18.7 1.0
N B:GLN429 4.9 14.2 1.0
O B:GLN429 4.9 13.9 1.0
CA B:SER432 5.0 20.6 1.0

Potassium binding site 3 out of 4 in 1pkx

Go back to Potassium Binding Sites List in 1pkx
Potassium binding site 3 out of 4 in the Crystal Structure of Human Atic in Complex with Xmp


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 Xmp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K2003

b:14.3
occ:1.00
 O C:THR428 2.6 14.3 1.0
O C:VAL425 2.7 17.3 1.0
O C:LEU589 2.8 14.7 1.0
OD1 C:ASP539 2.9 18.8 1.0
OG C:SER432 3.0 23.1 1.0
OG C:SER430 3.1 14.9 1.0
CB C:SER432 3.6 19.6 1.0
CB C:HIS591 3.6 17.5 1.0
C C:THR428 3.7 17.5 1.0
N C:HIS591 3.8 15.4 1.0
CG C:ASP539 3.8 17.6 1.0
CB C:ASP539 3.8 17.7 1.0
C C:VAL425 3.8 17.2 1.0
C C:LEU589 4.0 16.2 1.0
C C:PHE590 4.2 18.2 1.0
N C:SER430 4.2 16.9 1.0
N C:THR428 4.2 12.8 1.0
CB C:SER430 4.3 15.0 1.0
CA C:PHE590 4.3 17.1 1.0
CA C:HIS591 4.3 17.9 1.0
CA C:SER430 4.4 18.0 1.0
CA C:THR428 4.4 15.2 1.0
C C:GLN429 4.5 19.2 1.0
CB C:THR428 4.5 13.5 1.0
O C:LYS426 4.6 14.8 1.0
N C:PHE590 4.6 17.8 1.0
C C:LYS426 4.6 16.8 1.0
CG1 C:VAL425 4.6 21.7 1.0
O C:HOH2172 4.7 23.4 1.0
CA C:LYS426 4.7 17.5 1.0
N C:LYS426 4.7 16.0 1.0
CA C:VAL425 4.8 17.8 1.0
N C:GLN429 4.8 17.7 1.0
O C:GLN429 4.8 17.8 1.0
CG C:HIS591 4.8 18.1 1.0
O C:HIS591 4.8 17.9 1.0
CA C:SER432 4.9 19.3 1.0
CB C:LEU589 4.9 16.8 1.0
O C:PHE590 4.9 14.0 1.0
OD2 C:ASP539 5.0 19.2 1.0
CA C:GLN429 5.0 19.1 1.0
N C:SER432 5.0 16.9 1.0

Potassium binding site 4 out of 4 in 1pkx

Go back to Potassium Binding Sites List in 1pkx
Potassium binding site 4 out of 4 in the Crystal Structure of Human Atic in Complex with Xmp


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 Xmp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K2004

b:17.5
occ:1.00
 O D:THR428 2.7 18.0 1.0
O D:VAL425 2.7 17.4 1.0
O D:LEU589 2.7 14.2 1.0
OG D:SER432 2.8 22.9 1.0
OD1 D:ASP539 2.8 21.4 1.0
OG D:SER430 3.0 16.9 1.0
CB D:HIS591 3.6 16.6 1.0
CB D:SER432 3.7 20.6 1.0
N D:HIS591 3.7 16.9 1.0
CG D:ASP539 3.8 24.6 1.0
C D:VAL425 3.8 17.8 1.0
C D:THR428 3.8 13.8 1.0
CB D:ASP539 3.9 21.1 1.0
C D:LEU589 3.9 14.4 1.0
C D:PHE590 4.1 17.8 1.0
CA D:PHE590 4.2 15.2 1.0
CB D:SER430 4.2 17.2 1.0
N D:SER430 4.3 17.3 1.0
N D:THR428 4.3 16.5 1.0
CA D:HIS591 4.3 17.3 1.0
CA D:SER430 4.4 18.0 1.0
O D:HOH2163 4.4 30.3 1.0
CA D:THR428 4.5 14.7 1.0
CB D:THR428 4.5 15.3 1.0
C D:GLN429 4.5 17.9 1.0
N D:PHE590 4.5 14.8 1.0
CA D:VAL425 4.6 18.6 1.0
C D:LYS426 4.7 16.2 1.0
O D:LYS426 4.7 16.7 1.0
N D:LYS426 4.7 16.9 1.0
CB D:VAL425 4.7 20.2 1.0
N D:SER432 4.7 18.7 1.0
CA D:LYS426 4.7 15.6 1.0
O D:GLN429 4.8 15.0 1.0
CG D:HIS591 4.8 18.2 1.0
O D:HIS591 4.8 16.1 1.0
O D:PHE590 4.8 14.7 1.0
CA D:SER432 4.9 19.6 1.0
N D:GLN429 4.9 14.4 1.0
OD2 D:ASP539 4.9 22.2 1.0
CB D:LEU589 5.0 15.9 1.0

Reference:

D.W.Wolan, C.G.Cheong, S.E.Greasley, I.A.Wilson. Structural Insights Into the Human and Avian Imp Cyclohydrolase Mechanism Via Crystal Structures with the Bound Xmp Inhibitor. Biochemistry V. 43 1171 2004.
ISSN: ISSN 0006-2960
PubMed: 14756553
DOI: 10.1021/BI030162I
Page generated: Sun Dec 13 22:57:40 2020

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