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Magnesium in PDB 2pvf: Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide

Enzymatic activity of Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide

All present enzymatic activity of Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide, PDB code: 2pvf was solved by H.Chen, M.Mohammadi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.353, 78.436, 84.839, 90.00, 90.00, 90.00
R / Rfree (%) 25.1 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide (pdb code 2pvf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide, PDB code: 2pvf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2pvf

Go back to Magnesium Binding Sites List in 2pvf
Magnesium binding site 1 out of 2 in the Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide


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 Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:25.1
occ:1.00
 OD2 A:ASP644 2.2 19.8 1.0
ND2 A:ASN631 2.2 17.8 1.0
O2B A:ACP300 2.3 26.4 1.0
O B:HOH1 2.3 23.9 1.0
O A:HOH2 2.3 26.1 1.0
O2A A:ACP300 2.3 27.4 1.0
CG A:ASP644 3.2 19.6 1.0
CG A:ASN631 3.3 19.8 1.0
PB A:ACP300 3.3 27.0 1.0
PA A:ACP300 3.5 27.1 1.0
O3A A:ACP300 3.6 27.3 1.0
CB A:ASP644 3.6 19.5 1.0
OD1 A:ASN631 3.7 19.6 1.0
O A:HOH101 3.9 31.2 1.0
O1B A:ACP300 3.9 27.1 1.0
O A:HOH111 4.0 21.6 1.0
O A:HOH79 4.3 38.7 1.0
OD1 A:ASP644 4.3 19.3 1.0
O A:ARG630 4.3 21.6 1.0
O5' A:ACP300 4.4 27.5 1.0
C5' A:ACP300 4.5 27.3 1.0
OH B:TYR606 4.6 27.8 1.0
CB A:ASN631 4.6 19.4 1.0
O1A A:ACP300 4.6 28.0 1.0
C3B A:ACP300 4.7 28.9 1.0
CA A:ASN631 4.8 20.3 1.0
CD A:ARG630 4.9 22.7 1.0
C A:ARG630 4.9 21.2 1.0
CG A:ARG630 4.9 21.6 1.0
O A:HOH76 4.9 34.1 1.0

Magnesium binding site 2 out of 2 in 2pvf

Go back to Magnesium Binding Sites List in 2pvf
Magnesium binding site 2 out of 2 in the Crystal Structure of Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide


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 Tyrosine Phosphorylated Activated Fgf Receptor 2 (FGFR2) Kinase Domain in Complex with Atp Analog and Substrate Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:24.3
occ:1.00
 O A:HOH112 2.2 18.8 1.0
O1B A:ACP300 2.2 27.1 1.0
O A:HOH114 2.3 23.4 1.0
O A:HOH113 2.3 25.5 1.0
O2G A:ACP300 2.3 29.6 1.0
O A:HOH111 2.3 21.6 1.0
PB A:ACP300 3.3 27.0 1.0
PG A:ACP300 3.4 29.6 1.0
C3B A:ACP300 3.5 28.9 1.0
O2B A:ACP300 3.9 26.4 1.0
NZ A:LYS517 4.0 24.4 1.0
O A:HOH76 4.0 34.1 1.0
OD1 A:ASP644 4.1 19.3 1.0
OD2 A:ASP644 4.2 19.8 1.0
O1G A:ACP300 4.3 31.3 1.0
O A:HOH49 4.3 32.5 1.0
O3G A:ACP300 4.4 30.7 1.0
OE1 A:GLU534 4.5 22.8 1.0
CG A:ASP644 4.5 19.6 1.0
O3A A:ACP300 4.5 27.3 1.0
CE A:LYS517 4.6 25.1 1.0
O A:HOH19 4.7 25.3 1.0

Reference:

H.Chen, J.Ma, W.Li, A.V.Eliseenkova, C.Xu, T.A.Neubert, W.T.Miller, M.Mohammadi. A Molecular Brake in the Kinase Hinge Region Regulates the Activity of Receptor Tyrosine Kinases. Mol.Cell V. 27 717 2007.
ISSN: ISSN 1097-2765
PubMed: 17803937
DOI: 10.1016/J.MOLCEL.2007.06.028
Page generated: Wed Aug 14 02:18:39 2024

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