Chlorine in PDB 3ay9: Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State

The structure of Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State, PDB code: 3ay9 was solved by A.Arakawa, N.Handa, M.Shirouzu, S.Yokoyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.733, 61.343, 142.650, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 21.3

The structure of Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Potassium	(K)	1 atom
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State (pdb code 3ay9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State, PDB code: 3ay9:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human HSP70 Nbd in the Adp-, Mg Ion-, and K Ion- Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl6268 b:25.6 occ:1.00 NZ A:LYS345 3.1 26.2 1.0 O A:HOH451 3.1 26.5 1.0 O A:HOH450 3.1 24.7 1.0 NZ A:LYS348 3.2 22.5 1.0 CD A:LYS348 3.9 21.4 1.0 CD A:LYS345 3.9 25.0 1.0 CE A:LYS348 3.9 22.9 1.0 CE A:LYS345 4.0 26.7 1.0 CD2 A:LEU349 4.1 21.4 1.0 CG A:LYS348 4.3 19.7 1.0 OD2 A:ASP352 4.3 16.8 1.0 CG A:LEU349 4.4 20.3 1.0 O A:HOH443 4.4 29.2 1.0 CB A:LYS348 5.0 18.3 1.0

A.Arakawa, N.Handa, M.Shirouzu, S.Yokoyama. Biochemical and Structural Studies on the High Affinity of HSP70 For Adp. Protein Sci. V. 20 1367 2011.
ISSN: ISSN 0961-8368
PubMed: 21608060
DOI: 10.1002/PRO.663