Potassium in PDB 6jpt: Crystal Structure of Human PAC3 Homodimer (Trigonal Form)

Protein crystallography data

The structure of Crystal Structure of Human PAC3 Homodimer (Trigonal Form), PDB code: 6jpt was solved by T.Satoh, M.Yagi-Utsumi, K.Okamoto, E.Kurimoto, K.Tanaka, K.Kato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.66 / 0.96
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.229, 71.229, 47.074, 90.00, 90.00, 120.00
R / Rfree (%) 13.6 / 14.6

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human PAC3 Homodimer (Trigonal Form) (pdb code 6jpt). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Human PAC3 Homodimer (Trigonal Form), PDB code: 6jpt:

Potassium binding site 1 out of 1 in 6jpt

Go back to Potassium Binding Sites List in 6jpt
Potassium binding site 1 out of 1 in the Crystal Structure of Human PAC3 Homodimer (Trigonal Form)


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 PAC3 Homodimer (Trigonal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K202

b:35.5
occ:1.00
O A:HOH439 2.6 30.1 1.0
HE3 A:LYS102 2.7 27.0 1.0
HB1 A:ALA100 2.7 12.5 1.0
O A:HOH456 2.8 35.1 1.0
O A:HOH393 2.9 11.2 1.0
HA A:ALA100 3.0 11.7 1.0
HG3 A:LYS102 3.1 22.5 1.0
HD2 A:LYS41 3.3 22.3 1.0
CB A:ALA100 3.5 10.4 1.0
CA A:ALA100 3.6 9.7 1.0
CE A:LYS102 3.6 22.5 1.0
HB2 A:LYS41 3.7 14.7 1.0
HG2 A:LYS102 3.7 22.5 1.0
HD3 A:LYS41 3.8 22.3 1.0
CG A:LYS102 3.8 18.8 1.0
C A:ALA100 3.8 9.8 1.0
HB2 A:ALA100 3.8 12.5 1.0
HA2 A:GLY43 3.8 14.3 1.0
CD A:LYS41 4.0 18.6 1.0
HB3 A:LYS41 4.0 14.7 1.0
HE2 A:LYS102 4.0 27.0 1.0
N A:VAL101 4.2 10.3 1.0
H A:VAL101 4.2 12.3 1.0
HA3 A:GLY43 4.2 14.3 1.0
CB A:LYS41 4.3 12.2 1.0
O A:ALA100 4.3 10.9 1.0
CD A:LYS102 4.3 21.1 1.0
HB3 A:ALA100 4.3 12.5 1.0
O A:HOH346 4.4 11.6 1.0
HZ2 A:LYS102 4.5 27.9 1.0
CA A:GLY43 4.5 11.9 1.0
NZ A:LYS102 4.5 23.2 1.0
HZ1 A:LYS102 4.5 27.9 1.0
HD2 A:LYS102 4.5 25.4 1.0
O A:HOH413 4.6 35.3 1.0
O A:HOH364 4.7 19.8 1.0
H A:LYS102 4.7 14.2 1.0
CG A:LYS41 4.7 15.6 1.0
N A:LYS102 4.8 11.8 1.0
H A:GLY43 4.9 13.5 1.0
O A:HOH403 5.0 21.6 1.0
N A:ALA100 5.0 9.2 1.0
O A:HOH446 5.0 33.3 1.0
HA A:LYS102 5.0 16.5 1.0

Reference:

T.Satoh, M.Yagi-Utsumi, K.Okamoto, E.Kurimoto, K.Tanaka, K.Kato. Molecular and Structural Basis of the Proteasome Alpha Subunit Assembly Mechanism Mediated By the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer. Int J Mol Sci V. 20 2019.
ISSN: ESSN 1422-0067
PubMed: 31067643
DOI: 10.3390/IJMS20092231
Page generated: Mon Dec 14 00:44:01 2020

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