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Magnesium in PDB 4rix: Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R Mutation

Enzymatic activity of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R Mutation

All present enzymatic activity of Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R 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-Q790R Mutation, PDB code: 4rix 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) 59.77 / 3.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.649, 155.053, 86.857, 90.00, 111.09, 90.00
R / Rfree (%) 20.7 / 25.8

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-Q790R Mutation (pdb code 4rix). 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-Q790R Mutation, PDB code: 4rix:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4rix

Go back to Magnesium Binding Sites List in 4rix
Magnesium binding site 1 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R 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-Q790R Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:34.1
occ:1.00
 OD2 A:ASP833 2.1 65.1 1.0
OD1 A:ASN820 2.2 52.8 1.0
O3A A:ANP1101 2.4 83.5 1.0
N3B A:ANP1101 2.9 63.8 1.0
CG A:ASP833 3.0 70.5 1.0
PB A:ANP1101 3.1 66.5 1.0
O3G A:ANP1101 3.2 82.1 1.0
O2A A:ANP1101 3.3 77.3 1.0
CG A:ASN820 3.4 46.5 1.0
PA A:ANP1101 3.5 84.2 1.0
PG A:ANP1101 3.5 63.4 1.0
OD1 A:ASP833 3.6 91.4 1.0
O1B A:ANP1101 3.8 70.1 1.0
O1G A:ANP1101 3.9 71.8 1.0
CB A:ASP833 4.1 52.5 1.0
ND2 A:ASN820 4.2 55.8 1.0
NZ A:LYS723 4.3 51.3 1.0
O5' A:ANP1101 4.3 80.2 1.0
CB A:ASN820 4.4 35.9 1.0
CA A:ASN820 4.5 34.8 1.0
O2B A:ANP1101 4.5 90.7 1.0
O1A A:ANP1101 4.6 87.4 1.0
O A:ARG819 4.6 56.3 1.0
C8 A:ANP1101 4.9 66.2 1.0

Magnesium binding site 2 out of 4 in 4rix

Go back to Magnesium Binding Sites List in 4rix
Magnesium binding site 2 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R 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-Q790R Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1002

b:72.5
occ:1.00
 O1B B:ADP1001 2.3 0.7 1.0
OD1 B:ASN818 3.1 55.1 1.0
O2A B:ADP1001 3.4 0.4 1.0
PB B:ADP1001 3.7 0.7 1.0
CG B:ASN818 4.0 50.1 1.0
NE B:ARG817 4.0 54.2 1.0
ND2 B:ASN818 4.1 48.7 1.0
OD2 B:ASP813 4.1 57.4 1.0
O3B B:ADP1001 4.2 0.0 1.0
O3A B:ADP1001 4.4 0.9 1.0
OD2 B:ASP831 4.5 0.1 1.0
PA B:ADP1001 4.5 0.3 1.0
NH2 B:ARG817 4.6 56.4 1.0
CB B:ARG817 4.7 46.5 1.0
CD B:ARG817 4.8 64.7 1.0
CZ B:ARG817 4.8 52.1 1.0
O2B B:ADP1001 4.8 1.0 1.0
CG B:ASP831 4.9 96.9 1.0
OD1 B:ASP831 5.0 99.3 1.0

Magnesium binding site 3 out of 4 in 4rix

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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-Q790R 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-Q790R Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1102

b:20.4
occ:1.00
 OD2 C:ASP833 2.0 44.8 1.0
O3A C:ANP1101 2.2 67.1 1.0
OD1 C:ASN820 2.3 43.6 1.0
N3B C:ANP1101 2.5 51.9 1.0
O2A C:ANP1101 2.7 46.6 1.0
O3G C:ANP1101 2.8 46.4 1.0
PB C:ANP1101 2.8 39.5 1.0
PA C:ANP1101 3.0 44.1 1.0
CG C:ASP833 3.0 54.2 1.0
PG C:ANP1101 3.2 35.8 1.0
CG C:ASN820 3.5 40.8 1.0
OD1 C:ASP833 3.6 75.9 1.0
O1B C:ANP1101 3.7 50.8 1.0
O1A C:ANP1101 4.0 48.0 1.0
NZ C:LYS723 4.1 30.0 1.0
O2B C:ANP1101 4.1 42.1 1.0
CB C:ASP833 4.1 42.4 1.0
O5' C:ANP1101 4.2 60.6 1.0
O1G C:ANP1101 4.2 38.9 1.0
ND2 C:ASN820 4.2 43.6 1.0
O2G C:ANP1101 4.4 46.3 1.0
CB C:ASN820 4.5 40.4 1.0
CA C:ASN820 4.7 22.6 1.0
O C:ARG819 4.8 55.0 1.0
C8 C:ANP1101 4.8 50.7 1.0

Magnesium binding site 4 out of 4 in 4rix

Go back to Magnesium Binding Sites List in 4rix
Magnesium binding site 4 out of 4 in the Crystal Structure of An Egfr/HER3 Kinase Domain Heterodimer Containing the Cancer-Associated HER3-Q790R 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-Q790R Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1002

b:67.2
occ:1.00
 O2A D:ADP1001 2.4 0.5 1.0
OD1 D:ASN818 2.6 44.7 1.0
O2B D:ADP1001 2.9 0.3 1.0
CG D:ASN818 3.7 49.9 1.0
NE D:ARG817 3.8 67.3 1.0
PA D:ADP1001 3.8 0.3 1.0
CB D:ARG817 3.9 61.9 1.0
O3B D:ADP1001 3.9 0.0 1.0
PB D:ADP1001 3.9 0.3 1.0
ND2 D:ASN818 4.1 49.1 1.0
O5' D:ADP1001 4.2 1.0 1.0
C5' D:ADP1001 4.3 0.4 1.0
CD D:ARG817 4.3 74.9 1.0
O3A D:ADP1001 4.4 0.6 1.0
OD2 D:ASP831 4.5 85.1 1.0
C D:ARG817 4.6 59.2 1.0
O D:ARG817 4.7 52.9 1.0
CG D:ARG817 4.8 73.9 1.0
CZ D:ARG817 4.8 65.6 1.0
C4' D:ADP1001 4.8 0.3 1.0
N D:ASN818 4.9 65.6 1.0
NH2 D:ARG817 4.9 63.0 1.0
CA D:ARG817 4.9 57.8 1.0
CB D:ASN818 4.9 59.0 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 03:08:45 2024

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