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Sodium in PDB 5j28: KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex

Enzymatic activity of KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex

All present enzymatic activity of KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex:
3.1.3.16;

Protein crystallography data

The structure of KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex, PDB code: 5j28 was solved by G.S.Kumar, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.33 / 2.00
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 90.832, 90.832, 206.717, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 19.7

Sodium Binding Sites:

The binding sites of Sodium atom in the KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex (pdb code 5j28). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex, PDB code: 5j28:

Sodium binding site 1 out of 1 in 5j28

Go back to Sodium Binding Sites List in 5j28
Sodium binding site 1 out of 1 in the KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of KI67-PP1G (Protein Phosphatase 1, Gamma Isoform) Holoenzyme Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na402

b:46.5
occ:1.00
OE1 A:GLU167 2.7 43.2 1.0
OE2 A:GLU54 3.0 37.9 1.0
OE2 A:GLU167 3.4 42.8 1.0
CD1 A:ILE164 3.4 29.5 1.0
CD A:GLU167 3.5 35.6 1.0
OE1 A:GLU54 3.5 29.2 1.0
CD A:GLU54 3.6 31.0 1.0
NH2 A:ARG187 3.8 33.2 1.0
O A:HOH604 4.0 44.6 1.0
CB A:ILE164 4.4 21.4 1.0
CG2 A:ILE164 4.4 24.2 1.0
CG1 A:ILE164 4.5 23.8 1.0
O A:HOH589 4.7 43.8 1.0
CG A:GLU167 4.9 34.6 1.0
CG A:MET183 5.0 30.9 1.0

Reference:

G.S.Kumar, E.Gokhan, S.De Munter, M.Bollen, P.Vagnarelli, W.Peti, R.Page. The Ki-67 and Repoman Mitotic Phosphatases Assemble Via An Identical, Yet Novel Mechanism. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27572260
DOI: 10.7554/ELIFE.16539
Page generated: Mon Aug 18 00:25:08 2025

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