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Magnesium in PDB 7s9h: Cryogenic Human HSP90A-Ntd Bound to EC144

Enzymatic activity of Cryogenic Human HSP90A-Ntd Bound to EC144

All present enzymatic activity of Cryogenic Human HSP90A-Ntd Bound to EC144:
3.6.4.10;

Protein crystallography data

The structure of Cryogenic Human HSP90A-Ntd Bound to EC144, PDB code: 7s9h was solved by T.R.Stachowski, M.Vanarotti, J.Seetharaman, M.Fischer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.46 / 1.45
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 66.381, 90.196, 97.719, 90, 90, 90
R / Rfree (%) 15.7 / 18.4

Other elements in 7s9h:

The structure of Cryogenic Human HSP90A-Ntd Bound to EC144 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryogenic Human HSP90A-Ntd Bound to EC144 (pdb code 7s9h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryogenic Human HSP90A-Ntd Bound to EC144, PDB code: 7s9h:

Magnesium binding site 1 out of 1 in 7s9h

Go back to Magnesium Binding Sites List in 7s9h
Magnesium binding site 1 out of 1 in the Cryogenic Human HSP90A-Ntd Bound to EC144


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryogenic Human HSP90A-Ntd Bound to EC144 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:26.0
occ:1.00
H A:GLN23 2.1 29.1 1.0
HA A:PHE22 2.7 21.7 1.0
HD1 A:PHE22 2.8 20.8 1.0
N A:GLN23 2.9 24.2 1.0
HA3 A:GLY108 2.9 28.8 1.0
O A:HOH522 3.0 21.7 0.9
O A:HOH463 3.0 31.9 0.9
HG2 A:GLN23 3.3 49.6 1.0
HG3 A:GLN23 3.3 49.6 1.0
HB2 A:GLN23 3.4 39.5 1.0
HG13 A:ILE26 3.4 38.1 1.0
CA A:PHE22 3.5 18.1 1.0
HE1 A:PHE170 3.6 20.8 1.0
CG A:GLN23 3.6 41.3 1.0
HB3 A:PHE22 3.6 21.2 1.0
CD1 A:PHE22 3.7 17.3 1.0
C A:PHE22 3.7 22.5 1.0
HA2 A:GLY108 3.7 28.8 1.0
CA A:GLY108 3.8 24.0 1.0
HB A:ILE26 3.8 24.7 1.0
CB A:GLN23 3.8 32.9 1.0
CA A:GLN23 3.9 26.1 1.0
CB A:PHE22 4.0 17.6 1.0
HG21 A:ILE26 4.0 28.8 1.0
CG A:PHE22 4.2 15.3 1.0
CG1 A:ILE26 4.3 31.7 1.0
CE1 A:PHE170 4.3 17.3 1.0
CB A:ILE26 4.4 20.6 1.0
O A:HOH574 4.4 43.5 1.0
O A:ALA21 4.5 21.8 1.0
HA A:GLN23 4.6 31.3 1.0
O A:HOH557 4.6 28.6 0.8
HE1 A:PHE22 4.6 22.7 1.0
CG2 A:ILE26 4.6 24.0 1.0
CE1 A:PHE22 4.6 18.9 1.0
H A:GLY108 4.6 25.9 1.0
O A:HOH532 4.6 26.2 1.0
HG12 A:ILE26 4.7 38.1 1.0
C A:GLY108 4.7 19.5 1.0
N A:GLY108 4.7 21.6 1.0
N A:PHE22 4.7 19.8 1.0
HG22 A:ILE26 4.7 28.8 1.0
O A:HOH538 4.7 25.0 1.0
HB3 A:GLN23 4.7 39.5 1.0
HZ A:PHE170 4.8 20.8 1.0
O A:GLN23 4.9 23.0 1.0
HB2 A:PHE22 4.9 21.2 1.0
O A:PHE22 4.9 21.7 1.0
C A:GLN23 4.9 25.1 1.0
CZ A:PHE170 5.0 17.3 1.0
O A:GLY108 5.0 23.8 1.0

Reference:

T.R.Stachowski, M.Vanarotti, J.Seetharaman, K.Lopez, M.Fischer. Water Networks Repopulate Protein-Ligand Interfaces with Temperature. Angew.Chem.Int.Ed.Engl. V. 61 12919 2022.
ISSN: ESSN 1521-3773
PubMed: 35648650
DOI: 10.1002/ANIE.202112919
Page generated: Thu Oct 3 08:15:23 2024

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