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Magnesium in PDB 3gqi: Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates

Enzymatic activity of Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates

All present enzymatic activity of Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates:
2.7.10.1; 3.1.4.11;

Protein crystallography data

The structure of Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates, PDB code: 3gqi was solved by J.H.Bae, E.D.Lew, S.Yuzawa, F.Tome, I.Lax, J.Schlessinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 133.935, 64.596, 94.209, 90.00, 96.50, 90.00
R / Rfree (%) 24.9 / 28.9

Other elements in 3gqi:

The structure of Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates also contains other interesting chemical elements:

Vanadium (V) 10 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates (pdb code 3gqi). 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 Activated Receptor Tyrosine Kinase in Complex with Substrates, PDB code: 3gqi:

Magnesium binding site 1 out of 1 in 3gqi

Go back to Magnesium Binding Sites List in 3gqi
Magnesium binding site 1 out of 1 in the Crystal Structure of Activated Receptor Tyrosine Kinase in Complex with Substrates


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 Activated Receptor Tyrosine Kinase in Complex with Substrates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg776

b:74.8
occ:1.00
O2B A:ACP775 2.1 95.2 1.0
OD2 A:ASP641 2.4 60.2 1.0
OD1 A:ASN628 2.5 55.4 1.0
O1A A:ACP775 2.6 90.3 1.0
PB A:ACP775 3.2 95.1 1.0
CG A:ASN628 3.5 52.6 1.0
CG A:ASP641 3.6 58.1 1.0
O1B A:ACP775 3.6 95.5 1.0
ND2 A:ASN628 3.8 55.0 1.0
PA A:ACP775 3.9 91.3 1.0
CD A:ARG627 4.0 48.7 1.0
O3A A:ACP775 4.0 93.1 1.0
NE A:ARG627 4.0 51.5 1.0
CB A:ASP641 4.3 54.4 1.0
OD2 A:ASP623 4.4 51.5 1.0
OD1 A:ASP641 4.6 58.1 1.0
C5' A:ACP775 4.6 87.4 1.0
O1G A:ACP775 4.6 94.3 1.0
CG A:ARG627 4.7 48.0 1.0
C3B A:ACP775 4.7 95.4 1.0
O5' A:ACP775 4.7 89.3 1.0
O A:ARG627 4.8 44.9 1.0
CB A:ASN628 4.9 50.4 1.0
O2A A:ACP775 5.0 89.4 1.0

Reference:

J.H.Bae, E.D.Lew, S.Yuzawa, F.Tome, I.Lax, J.Schlessinger. The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled By A Secondary SH2 Domain Binding Site. Cell(Cambridge,Mass.) V. 138 514 2009.
ISSN: ISSN 0092-8674
PubMed: 19665973
DOI: 10.1016/J.CELL.2009.05.028
Page generated: Mon Dec 14 08:12:06 2020

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