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Sodium in PDB 4zqk: Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1.

Protein crystallography data

The structure of Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1., PDB code: 4zqk was solved by K.M.Zak, G.Dubin, T.A.Holak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.37 / 2.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.862, 70.862, 114.367, 90.00, 90.00, 120.00
R / Rfree (%) 20.7 / 25.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1. (pdb code 4zqk). 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 Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1., PDB code: 4zqk:

Sodium binding site 1 out of 1 in 4zqk

Go back to Sodium Binding Sites List in 4zqk
Sodium binding site 1 out of 1 in the Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the Complex of Human Programmed Death-1 (Pd-1) and Its Ligand Pd-L1. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na201

b:50.1
occ:1.00
NH1 A:ARG86 3.5 58.3 1.0
N A:LYS89 3.8 42.5 1.0
NH2 A:ARG86 4.0 63.5 1.0
N A:ASP90 4.2 50.4 1.0
CZ A:ARG86 4.2 59.6 1.0
CA A:LEU88 4.4 45.4 1.0
C A:LEU88 4.4 40.8 1.0
CG A:ASP90 4.4 60.9 1.0
OD1 A:ASP90 4.5 68.1 1.0
CB A:LYS89 4.5 49.9 1.0
CA A:LYS89 4.5 47.8 1.0
CD2 A:LEU88 4.5 49.4 1.0
OD2 A:ASP90 4.6 60.6 1.0
CB A:LEU88 4.8 44.7 1.0
CB A:ASP90 4.8 53.9 1.0
C A:LYS89 4.9 46.5 1.0

Reference:

K.M.Zak, R.Kitel, S.Przetocka, P.Golik, K.Guzik, B.Musielak, A.Domling, G.Dubin, T.A.Holak. Structure of the Complex of Human Programmed Death 1, Pd-1, and Its Ligand Pd-L1. Structure V. 23 2341 2015.
ISSN: ISSN 0969-2126
PubMed: 26602187
DOI: 10.1016/J.STR.2015.09.010
Page generated: Tue Dec 15 10:10:09 2020

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