Nickel in PDB 1sf8: Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90

The structure of Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90, PDB code: 1sf8 was solved by S.F.Harris, A.K.Shiau, D.A.Agard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.90 / 2.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.516, 103.516, 249.738, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 26.1

The structure of Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90 also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Nickel atom in the Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90 (pdb code 1sf8). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 3 binding sites of Nickel where determined in the Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90, PDB code: 1sf8:
Jump to Nickel binding site number: 1; 2; 3;

Nickel binding site 1 out of 3 in the Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90 within 5.0Å range: probe atom residue distance (Å) B Occ C:Ni700 b:86.5 occ:1.00 OD1 C:ASP573 2.2 76.3 1.0 NE2 C:HIS530 2.6 65.4 1.0 NE2 C:HIS507 2.7 0.5 1.0 CD2 C:HIS505 2.8 0.1 1.0 NE2 C:HIS505 3.1 0.9 1.0 CG C:ASP573 3.1 74.0 1.0 CE1 C:HIS507 3.2 0.9 1.0 OD2 C:ASP573 3.4 76.4 1.0 O C:HIS505 3.4 0.5 1.0 CE1 C:HIS530 3.5 65.9 1.0 CD2 C:HIS530 3.6 64.7 1.0 CD2 C:HIS507 3.7 0.9 1.0 CG C:HIS505 3.7 0.2 1.0 CE1 C:HIS505 4.0 0.1 1.0 CB C:PRO572 4.1 64.9 1.0 ND1 C:HIS507 4.2 0.4 1.0 ND1 C:HIS505 4.3 0.3 1.0 C C:HIS505 4.5 0.8 1.0 N C:ASP573 4.5 66.5 1.0 CB C:ASP573 4.5 70.9 1.0 CG C:HIS507 4.5 0.6 1.0 ND1 C:HIS530 4.6 66.5 1.0 CB C:HIS505 4.6 0.5 1.0 CG C:HIS530 4.6 65.0 1.0 CA C:ASP573 4.8 68.0 1.0 CA C:HIS505 4.9 0.6 1.0 CG C:PRO572 5.0 65.4 1.0 C C:PRO572 5.0 65.5 1.0

Nickel binding site 2 out of 3 in the Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90 within 5.0Å range: probe atom residue distance (Å) B Occ D:Ni701 b:78.8 occ:1.00 OD1 D:ASP573 2.2 81.2 1.0 NE2 D:HIS530 2.2 77.4 1.0 OD2 D:ASP573 2.3 77.8 1.0 CE1 D:HIS530 2.4 78.3 1.0 CG D:ASP573 2.5 79.0 1.0 CD2 D:HIS530 3.6 78.5 1.0 ND1 D:HIS530 3.7 78.9 1.0 CB D:ASP573 4.0 77.1 1.0 CG D:HIS530 4.3 79.4 1.0 N D:ASP573 4.4 74.9 1.0 CB D:PRO572 4.4 74.2 1.0 CA D:ASP573 4.6 76.0 1.0 C D:PRO572 4.9 74.5 1.0

Nickel binding site 3 out of 3 in the Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Crystal Structure of the Carboxy-Terminal Domain of Htpg, the E. Coli HSP90 within 5.0Å range: probe atom residue distance (Å) B Occ G:Ni702 b:40.8 occ:1.00 OD1 G:ASP573 1.9 41.4 1.0 NE2 G:HIS530 2.0 41.4 1.0 ND1 G:HIS505 2.1 76.5 1.0 NE2 G:HIS507 2.1 68.4 1.0 CE1 G:HIS507 2.7 68.4 1.0 CG G:ASP573 2.8 41.7 1.0 CE1 G:HIS505 2.9 77.2 1.0 CD2 G:HIS530 2.9 36.4 1.0 OD2 G:ASP573 3.0 44.0 1.0 CE1 G:HIS530 3.0 37.0 1.0 CG G:HIS505 3.1 77.8 1.0 CD2 G:HIS507 3.3 70.7 1.0 CB G:HIS505 3.5 81.2 1.0 NE2 G:HIS505 4.0 77.6 1.0 ND1 G:HIS507 4.0 69.4 1.0 CG G:HIS530 4.1 35.9 1.0 CD2 G:HIS505 4.1 77.3 1.0 ND1 G:HIS530 4.1 36.1 1.0 CB G:ASP573 4.2 40.7 1.0 CG G:HIS507 4.3 71.4 1.0 CA G:HIS505 4.3 83.2 1.0 O G:HIS505 4.3 84.1 1.0 CB G:PRO572 4.4 35.8 1.0 N G:ASP573 4.5 37.5 1.0 CA G:ASP573 4.6 39.3 1.0 O G:HOH906 4.7 49.8 1.0 C G:HIS505 4.8 83.3 1.0 C G:PRO572 4.8 36.9 1.0 O G:HOH1118 5.0 70.8 1.0

S.F.Harris, A.K.Shiau, D.A.Agard. The Crystal Structure of the Carboxy-Terminal Dimerization Domain of Htpg, the Escherichia Coli HSP90, Reveals A Potential Substrate Binding Site. Structure V. 12 1087 2004.
ISSN: ISSN 0969-2126
PubMed: 15274928
DOI: 10.1016/J.STR.2004.03.020