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Magnesium in PDB 7oik: Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized

Enzymatic activity of Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized

All present enzymatic activity of Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized:
2.3.2.23; 2.3.2.27;

Other elements in 7oik:

The structure of Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized (pdb code 7oik). 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 Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized, PDB code: 7oik:

Magnesium binding site 1 out of 1 in 7oik

Go back to Magnesium Binding Sites List in 7oik
Magnesium binding site 1 out of 1 in the Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mouse RNF213:UBE2L3 Transthiolation Intermediate, Chemically Stabilized within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5202

b:180.5
occ:1.00
O2B A:ATP5201 2.1 176.4 1.0
OE2 A:GLU2060 2.2 175.7 1.0
OG A:SER1961 2.4 181.3 1.0
O2G A:ATP5201 2.5 176.4 1.0
CD A:GLU2060 3.1 175.7 1.0
O3B A:ATP5201 3.2 176.4 1.0
PB A:ATP5201 3.3 176.4 1.0
OE1 A:GLU2060 3.3 175.7 1.0
CB A:SER1961 3.4 181.3 1.0
PG A:ATP5201 3.5 176.4 1.0
O1A A:ATP5201 3.9 176.4 1.0
N A:SER1961 4.1 181.3 1.0
O3A A:ATP5201 4.1 176.4 1.0
NZ A:LYS2460 4.2 169.8 1.0
CA A:SER1961 4.3 181.3 1.0
O1G A:ATP5201 4.4 176.4 1.0
O1B A:ATP5201 4.4 176.4 1.0
CG A:GLU2060 4.5 175.7 1.0
PA A:ATP5201 4.5 176.4 1.0
O3G A:ATP5201 4.6 176.4 1.0
OD2 A:ASP2465 4.6 184.2 1.0
CB A:LYS1960 4.7 178.8 1.0
CE A:LYS1960 4.8 178.8 1.0
OD1 A:ASP2019 4.9 182.3 1.0

Reference:

J.Ahel, A.J.Fletcher, D.Grabarczyk, E.Roitinger, L.Deszcz, A.Lehner, S.Virdee, T.Clausen. E3 Ubiquitin Ligase RNF213 Employs A Non-Canonical Zinc Finger Active Site and Is Allosterically Regulated By Atp To Be Published.
Page generated: Thu Oct 3 03:03:00 2024

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