Magnesium in PDB 6cjj: Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp

The structure of Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp, PDB code: 6cjj was solved by A.Hutchinson, P.Loppnau, C.Bountra, A.M.Edwards, C.H.Arrowsmith, R.Hui, S.G.C.Structural Genomics Consortium, J.C.Pizarro, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.74
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.088, 74.088, 107.873, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19

The binding sites of Magnesium atom in the Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp (pdb code 6cjj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp, PDB code: 6cjj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:24.4 occ:1.00 OD1 A:ASN40 2.0 23.0 1.0 O1A A:ADP303 2.0 22.9 1.0 O3B A:ADP303 2.0 25.4 1.0 O A:HOH536 2.2 22.0 1.0 O A:HOH416 2.2 24.4 1.0 O A:HOH519 2.3 26.3 1.0 CG A:ASN40 3.0 23.0 1.0 HD21 A:ASN40 3.0 25.9 1.0 PB A:ADP303 3.1 26.8 1.0 PA A:ADP303 3.1 24.8 1.0 O3A A:ADP303 3.3 24.1 1.0 ND2 A:ASN40 3.4 21.6 1.0 O2B A:ADP303 3.6 26.3 1.0 O5' A:ADP303 3.9 23.7 1.0 HA3 A:GLY126 3.9 28.0 1.0 O A:HOH449 3.9 21.9 1.0 H A:GLY126 4.0 28.7 1.0 O A:HOH429 4.0 33.4 1.0 HA A:ASN40 4.1 23.0 1.0 H A:PHE127 4.2 24.4 1.0 HD22 A:ASN40 4.2 25.9 1.0 OE1 A:GLU36 4.3 27.4 1.0 CB A:ASN40 4.3 19.9 1.0 O1B A:ADP303 4.4 26.0 1.0 O2A A:ADP303 4.4 25.8 1.0 O A:HOH490 4.5 41.3 1.0 O A:GLU36 4.5 20.0 1.0 H3' A:ADP303 4.5 32.1 1.0 N A:GLY126 4.5 23.9 1.0 CA A:ASN40 4.6 19.1 1.0 CA A:GLY126 4.6 23.4 1.0 N A:PHE127 4.6 20.4 1.0 H A:ASN40 4.6 23.0 1.0 N A:ASN40 4.7 19.1 1.0 OD2 A:ASP43 4.7 24.0 1.0 HG A:SER39 4.7 30.3 0.3 HB3 A:SER39 4.8 28.1 0.3 HB3 A:ASN40 4.8 23.9 1.0 HB2 A:SER39 4.8 27.9 0.7 C A:GLY126 4.8 21.4 1.0 OG A:SER39 4.9 25.2 0.3 HB2 A:ASN40 4.9 23.9 1.0 HB3 A:GLU36 4.9 25.9 1.0 HB2 A:PHE127 5.0 26.5 1.0 HB3 A:SER39 5.0 27.9 0.7

Magnesium binding site 2 out of 2 in the Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Candida Albicans HSP90 Nucleotide Binding Domain in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:49.1 occ:1.00 OD1 A:ASP145 2.8 28.6 1.0 O A:HOH460 2.9 29.0 1.0 HE1 A:HIS143 3.2 28.8 1.0 HB2 A:ASN144 3.2 26.6 1.0 OE1 A:GLN58 3.3 25.4 1.0 O A:HOH590 3.4 46.5 1.0 CG A:ASP145 3.5 30.2 1.0 OD2 A:ASP145 3.6 28.1 1.0 O A:HOH512 3.7 39.3 1.0 HB3 A:ASN144 3.9 26.6 1.0 CE1 A:HIS143 4.0 24.0 1.0 CB A:ASN144 4.0 22.2 1.0 HD22 A:ASN144 4.0 25.7 1.0 OE1 A:GLN51 4.1 27.8 1.0 CD A:GLN58 4.1 30.5 1.0 O A:HOH565 4.1 37.8 1.0 HE22 A:GLN58 4.2 36.6 1.0 HE22 A:GLN51 4.5 33.4 1.0 H A:ASP145 4.5 25.9 1.0 NE2 A:GLN58 4.5 30.5 1.0 N A:ASP145 4.6 21.6 1.0 ND1 A:HIS143 4.6 22.2 1.0 CB A:ASP145 4.7 24.6 1.0 ND2 A:ASN144 4.8 21.4 1.0 C A:ASN144 4.8 23.6 1.0 HA A:ASP145 4.9 29.8 1.0 CA A:ASN144 4.9 20.6 1.0 HB2 A:ASP145 4.9 29.5 1.0 NE2 A:HIS143 4.9 22.5 1.0 HG3 A:GLN58 5.0 31.0 1.0 CG A:ASN144 5.0 23.2 1.0 CD A:GLN51 5.0 25.1 1.0

L.Whitesell, N.Robbins, D.S.Huang, C.A.Mclellan, T.Shekhar-Guturja, E.V.Leblanc, C.S.Nation, R.Hui, A.Hutchinson, C.Collins, S.Chatterjee, R.Trilles, J.L.Xie, D.J.Krysan, S.Lindquist, J.A.Porco Jr., U.Tatu, L.E.Brown, J.Pizarro, L.E.Cowen. Structural Basis For Species-Selective Targeting of HSP90 in A Pathogenic Fungus. Nat Commun V. 10 402 2019.
ISSN: ESSN 2041-1723
PubMed: 30679438
DOI: 10.1038/S41467-018-08248-W