Magnesium in PDB 7klv: Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp

Enzymatic activity of Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp

All present enzymatic activity of Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp:
1.3.5.1;

Other elements in 7klv:

The structure of Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp also contains other interesting chemical elements:

Potassium (K) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp (pdb code 7klv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp, PDB code: 7klv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7klv

Go back to Magnesium Binding Sites List in 7klv
Magnesium binding site 1 out of 2 in the Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:52.0
occ:1.00
OD1 A:ASN119 2.0 49.6 1.0
O3G A:ANP901 2.0 52.9 1.0
O1B A:ANP901 2.0 52.9 1.0
O2A A:ANP901 2.2 52.9 1.0
CG A:ASN119 3.0 49.6 1.0
PB A:ANP901 3.4 52.9 1.0
ND2 A:ASN119 3.5 49.6 1.0
PG A:ANP901 3.5 52.9 1.0
PA A:ANP901 3.5 52.9 1.0
O3A A:ANP901 3.9 52.9 1.0
O A:GLU115 4.0 48.8 1.0
N3B A:ANP901 4.1 52.9 1.0
OE2 A:GLU115 4.1 48.8 1.0
O2G A:ANP901 4.2 52.9 1.0
O1A A:ANP901 4.3 52.9 1.0
CB A:ASN119 4.3 49.6 1.0
CA A:GLY204 4.4 49.8 1.0
N A:ASN119 4.5 49.6 1.0
O1G A:ANP901 4.5 52.9 1.0
O2B A:ANP901 4.5 52.9 1.0
CA A:ASN119 4.6 49.6 1.0
C A:GLY204 4.7 49.8 1.0
O5' A:ANP901 4.7 52.9 1.0
C A:GLU115 4.8 48.8 1.0
N A:GLY204 4.8 49.8 1.0
N A:PHE205 4.8 49.4 1.0
CA A:GLY199 4.9 55.7 1.0
CB A:GLU115 4.9 48.8 1.0
CB A:SER118 4.9 48.2 1.0
CA A:GLU115 5.0 48.8 1.0

Magnesium binding site 2 out of 2 in 7klv

Go back to Magnesium Binding Sites List in 7klv
Magnesium binding site 2 out of 2 in the Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Full-Length Human Mitochondrial HSP90 (TRAP1) Spycatcher/Spytag-Sdhb Heterodimer in the Presence of Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg902

b:54.3
occ:1.00
OD1 B:ASN119 2.0 51.1 1.0
O3G B:ANP901 2.0 58.7 1.0
O2A B:ANP901 2.1 58.7 1.0
O1B B:ANP901 2.1 58.7 1.0
CG B:ASN119 3.0 51.1 1.0
PB B:ANP901 3.5 58.7 1.0
ND2 B:ASN119 3.5 51.1 1.0
PG B:ANP901 3.5 58.7 1.0
PA B:ANP901 3.6 58.7 1.0
O B:GLU115 4.0 50.6 1.0
O3A B:ANP901 4.0 58.7 1.0
OE1 B:GLU115 4.1 50.6 1.0
N3B B:ANP901 4.2 58.7 1.0
O1G B:ANP901 4.3 58.7 1.0
CB B:ASN119 4.3 51.1 1.0
CA B:GLY204 4.4 51.9 1.0
N B:ASN119 4.4 51.1 1.0
O1A B:ANP901 4.5 58.7 1.0
O2G B:ANP901 4.5 58.7 1.0
O5' B:ANP901 4.5 58.7 1.0
CA B:ASN119 4.5 51.1 1.0
O2B B:ANP901 4.6 58.7 1.0
C B:GLY204 4.7 51.9 1.0
C B:GLU115 4.8 50.6 1.0
CB B:SER118 4.8 48.3 1.0
CA B:GLY199 4.8 61.3 1.0
NH2 B:ARG402 4.9 60.8 1.0
N B:GLY204 4.9 51.9 1.0
N B:PHE205 5.0 50.9 1.0

Reference:

Y.X.Liu, D.A.Agard, D.Elnatan, M.Sun, A.G.Larson. Cryo-Em Analysis of Human Mitochondrial HSP90 in Multiple Tetrameric States To Be Published.
Page generated: Fri Nov 5 15:14:38 2021

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy