Zinc in PDB 4l3j: Crystal Structures of Human P70S6K1 Kinase Domain

The structure of Crystal Structures of Human P70S6K1 Kinase Domain, PDB code: 4l3j was solved by J.Wang, C.Zhong, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.511, 70.511, 150.484, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.5

The structure of Crystal Structures of Human P70S6K1 Kinase Domain also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Zinc atom in the Crystal Structures of Human P70S6K1 Kinase Domain (pdb code 4l3j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structures of Human P70S6K1 Kinase Domain, PDB code: 4l3j:

Zinc binding site 1 out of 1 in the Crystal Structures of Human P70S6K1 Kinase Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of Human P70S6K1 Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:43.5 occ:1.00 ND1 A:HIS228 2.1 55.3 1.0 ND1 A:HIS222 2.2 73.6 1.0 SG A:CYS217 2.3 51.3 1.0 SG A:CYS231 2.3 53.9 1.0 CE1 A:HIS228 3.0 57.5 1.0 CE1 A:HIS222 3.0 74.7 1.0 CB A:CYS217 3.0 56.3 1.0 CB A:CYS231 3.2 56.6 1.0 CG A:HIS228 3.3 64.1 1.0 CG A:HIS222 3.4 80.1 1.0 CB A:HIS228 3.7 71.0 1.0 CB A:HIS222 3.9 86.0 1.0 CA A:HIS222 3.9 88.5 1.0 NE2 A:HIS228 4.1 54.1 1.0 NE2 A:HIS222 4.2 73.8 1.0 CA A:HIS228 4.2 72.6 1.0 CD2 A:HIS228 4.3 59.4 1.0 CD2 A:HIS222 4.4 75.6 1.0 CA A:CYS217 4.5 56.6 1.0 N A:HIS222 4.6 94.7 1.0 CA A:CYS231 4.6 55.8 1.0 O A:HIS228 4.7 65.8 1.0 CB A:GLU219 4.7 56.8 1.0 C A:HIS222 4.9 88.2 1.0 CG A:GLU219 4.9 55.2 1.0 C A:HIS228 5.0 67.8 1.0

J.Wang, C.Zhong, F.Wang, F.Qu, J.Ding. Crystal Structures of S6K1 Provide Insights Into the Regulation Mechanism of S6K1 By the Hydrophobic Motif Biochem.J. V. 454 39 2013.
ISSN: ISSN 0264-6021
PubMed: 23731517
DOI: 10.1042/BJ20121863