Atomistry » Magnesium » PDB 4rcy-4rke » 4riy
Atomistry »
  Magnesium »
    PDB 4rcy-4rke »
      4riy »

Magnesium in PDB 4riy: Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation

Enzymatic activity of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation

All present enzymatic activity of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation, PDB code: 4riy was solved by P.Littlefield, L.Liu, N.Jura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.20 / 2.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 65.334, 155.140, 87.297, 90.00, 110.93, 90.00
R / Rfree (%) 21.6 / 26.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation (pdb code 4riy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation, PDB code: 4riy:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4riy

Go back to Magnesium Binding Sites List in 4riy
Magnesium binding site 1 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation


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 An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:23.3
occ:1.00
 OD2 A:ASP833 2.0 47.2 1.0
OD1 A:ASN820 2.3 40.6 1.0
O3A A:ANP1101 2.4 89.5 1.0
O2A A:ANP1101 2.7 39.5 1.0
O3G A:ANP1101 2.8 62.6 1.0
CG A:ASP833 3.0 43.6 1.0
N3B A:ANP1101 3.0 59.8 1.0
PA A:ANP1101 3.2 41.8 1.0
PB A:ANP1101 3.3 25.9 1.0
PG A:ANP1101 3.3 42.6 1.0
CG A:ASN820 3.5 41.6 1.0
OD1 A:ASP833 3.6 51.4 1.0
O1G A:ANP1101 3.7 49.4 1.0
NZ A:LYS723 3.9 43.5 1.0
CB A:ASP833 4.0 32.7 1.0
ND2 A:ASN820 4.1 49.0 1.0
O5' A:ANP1101 4.2 55.0 1.0
O1B A:ANP1101 4.2 32.6 1.0
O1A A:ANP1101 4.3 47.6 1.0
O2B A:ANP1101 4.5 76.2 1.0
CB A:ASN820 4.6 37.1 1.0
O2G A:ANP1101 4.8 27.5 1.0
CA A:ASN820 4.9 31.8 1.0

Magnesium binding site 2 out of 4 in 4riy

Go back to Magnesium Binding Sites List in 4riy
Magnesium binding site 2 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1002

b:60.9
occ:1.00
 OD1 B:ASN818 2.8 37.7 1.0
O2B B:ADP1001 2.9 0.4 1.0
O1B B:ADP1001 3.2 0.9 1.0
O2A B:ADP1001 3.3 0.0 1.0
PB B:ADP1001 3.5 0.2 1.0
CG B:ASN818 3.8 37.1 1.0
O3A B:ADP1001 4.1 0.4 1.0
ND2 B:ASN818 4.1 36.9 1.0
OD2 B:ASP831 4.2 90.1 1.0
PA B:ADP1001 4.3 0.1 1.0
OD2 B:ASP813 4.3 60.5 1.0
NE B:ARG817 4.4 32.3 1.0
CG B:ASP831 4.5 87.6 1.0
OD1 B:ASP831 4.5 89.9 1.0
C5' B:ADP1001 4.8 82.1 1.0
CB B:ARG817 4.8 32.8 1.0
O3B B:ADP1001 5.0 0.4 1.0

Magnesium binding site 3 out of 4 in 4riy

Go back to Magnesium Binding Sites List in 4riy
Magnesium binding site 3 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1102

b:17.3
occ:1.00
 OD2 C:ASP833 2.4 30.6 1.0
O2A C:ANP1101 2.4 31.4 1.0
OD1 C:ASN820 2.5 29.8 1.0
O3A C:ANP1101 2.5 67.2 1.0
N3B C:ANP1101 2.5 38.1 1.0
PA C:ANP1101 3.0 34.2 1.0
PB C:ANP1101 3.0 17.3 1.0
O3G C:ANP1101 3.1 26.9 1.0
CG C:ASP833 3.3 37.9 1.0
PG C:ANP1101 3.4 25.0 1.0
CG C:ASN820 3.6 29.8 1.0
OD1 C:ASP833 3.8 54.2 1.0
NZ C:LYS723 4.0 34.7 1.0
O1B C:ANP1101 4.0 19.2 1.0
O1A C:ANP1101 4.1 34.1 1.0
O5' C:ANP1101 4.1 47.1 1.0
O2B C:ANP1101 4.2 79.7 1.0
O1G C:ANP1101 4.3 30.2 1.0
CB C:ASP833 4.4 32.0 1.0
ND2 C:ASN820 4.4 31.8 1.0
O2G C:ANP1101 4.6 26.4 1.0
CB C:ASN820 4.7 25.8 1.0
C8 C:ANP1101 4.7 32.3 1.0
CA C:ASN820 4.9 17.6 1.0
O C:ARG819 4.9 30.8 1.0
C2' C:ANP1101 5.0 26.2 1.0

Magnesium binding site 4 out of 4 in 4riy

Go back to Magnesium Binding Sites List in 4riy
Magnesium binding site 4 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-E909G Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1002

b:59.3
occ:1.00
 O2B D:ADP1001 2.2 0.1 1.0
OD1 D:ASN818 2.4 48.2 1.0
O2A D:ADP1001 2.7 0.6 1.0
CG D:ASN818 3.5 44.6 1.0
PB D:ADP1001 3.7 0.7 1.0
ND2 D:ASN818 3.9 45.8 1.0
PA D:ADP1001 3.9 0.8 1.0
NE D:ARG817 4.1 49.0 1.0
CB D:ARG817 4.1 49.0 1.0
O5' D:ADP1001 4.3 70.2 1.0
O3A D:ADP1001 4.3 0.0 1.0
O3B D:ADP1001 4.3 0.7 1.0
OD2 D:ASP831 4.5 90.7 1.0
C5' D:ADP1001 4.6 69.5 1.0
C D:ARG817 4.7 40.4 1.0
CD D:ARG817 4.7 55.7 1.0
CB D:ASN818 4.8 44.5 1.0
O1B D:ADP1001 4.8 0.5 1.0
CG D:ASP831 4.8 87.8 1.0
O D:ARG817 4.8 33.7 1.0
OD2 D:ASP813 4.8 49.9 1.0
N D:ASN818 4.8 40.7 1.0
CA D:ASN818 4.9 43.9 1.0

Reference:

P.Littlefield, L.Liu, V.Mysore, Y.Shan, D.E.Shaw, N.Jura. Structural Analysis of the Egfr/HER3 Heterodimer Reveals the Molecular Basis For Activating HER3 Mutations. Sci.Signal. V. 7 RA114 2014.
ISSN: ESSN 1937-9145
PubMed: 25468994
DOI: 10.1126/SCISIGNAL.2005786
Page generated: Tue Aug 20 03:09:24 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy