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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

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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

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