Atomistry » Magnesium » PDB 6akp-6asw » 6ao5
Atomistry »
  Magnesium »
    PDB 6akp-6asw »
      6ao5 »

Magnesium in PDB 6ao5: Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain

Enzymatic activity of Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain

All present enzymatic activity of Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain, PDB code: 6ao5 was solved by D.R.Tomchick, X.Luo, L.Ni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.27 / 2.96
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 223.678, 223.678, 79.645, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 25.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain (pdb code 6ao5). 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 Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain, PDB code: 6ao5:

Magnesium binding site 1 out of 1 in 6ao5

Go back to Magnesium Binding Sites List in 6ao5
Magnesium binding site 1 out of 1 in the Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human MST2 in Complex with SAV1 Sarah Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:30.6
occ:1.00
O1B A:ANP501 2.2 37.7 1.0
OD2 A:ASP164 2.2 45.8 1.0
OD1 A:ASN151 2.3 23.3 1.0
O1G A:ANP501 2.6 34.9 1.0
O1A A:ANP501 2.7 48.1 1.0
HA A:ASN151 3.3 28.3 1.0
CG A:ASP164 3.4 45.8 1.0
CG A:ASN151 3.5 22.8 1.0
O5' A:ANP501 3.5 34.0 1.0
PB A:ANP501 3.6 36.7 1.0
PA A:ANP501 3.6 47.9 1.0
O A:GLY150 3.7 23.2 1.0
HZ3 A:LYS56 3.7 79.3 1.0
H8 A:ANP501 3.8 33.6 1.0
PG A:ANP501 4.0 34.5 1.0
CA A:ASN151 4.1 23.2 1.0
HB2 A:ASP164 4.1 54.4 1.0
H3' A:ANP501 4.1 43.7 1.0
OD1 A:ASP164 4.2 46.5 1.0
O3A A:ANP501 4.2 0.5 1.0
CB A:ASN151 4.3 22.9 1.0
C A:GLY150 4.3 22.5 1.0
HD21 A:LEU153 4.3 30.1 1.0
CB A:ASP164 4.4 44.9 1.0
N3B A:ANP501 4.4 85.2 1.0
N A:ASN151 4.4 22.7 1.0
ND2 A:ASN151 4.5 22.3 1.0
HB3 A:ALA163 4.5 27.7 1.0
HD21 A:ASN151 4.5 27.2 1.0
HB3 A:ASN151 4.5 27.9 1.0
C8 A:ANP501 4.5 27.6 1.0
HZ1 A:LYS56 4.5 79.3 1.0
NZ A:LYS56 4.5 65.7 1.0
O2G A:ANP501 4.5 0.5 1.0
O2B A:ANP501 4.6 35.1 1.0
HNB1 A:ANP501 4.6 0.8 1.0
HB3 A:ASP164 4.8 54.4 1.0
C5' A:ANP501 4.8 34.2 1.0
HD11 A:LEU153 4.8 31.6 1.0
HB1 A:ALA163 4.9 27.7 1.0
HZ2 A:LYS56 4.9 79.3 1.0
C3' A:ANP501 5.0 36.0 1.0

Reference:

S.J.Bae, L.Ni, A.Osinski, D.R.Tomchick, C.A.Brautigam, X.Luo. SAV1 Promotes Hippo Kinase Activation Through Antagonizing the PP2A Phosphatase Stripak. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 29063833
DOI: 10.7554/ELIFE.30278
Page generated: Mon Sep 30 19:15:31 2024

Last articles

Ca in 2XGQ
Ca in 2XHN
Ca in 2XGP
Ca in 2XJ7
Ca in 2XHI
Ca in 2XHJ
Ca in 2XHH
Ca in 2XF2
Ca in 2XFV
Ca in 2XFG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy