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Magnesium in PDB 4lmn: Crystal Structure of MEK1 Kinase Bound to GDC0973

Enzymatic activity of Crystal Structure of MEK1 Kinase Bound to GDC0973

All present enzymatic activity of Crystal Structure of MEK1 Kinase Bound to GDC0973:
2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of MEK1 Kinase Bound to GDC0973, PDB code: 4lmn was solved by M.H.Ultsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.69 / 2.80
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 81.610, 81.610, 129.809, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 23.3

Other elements in 4lmn:

The structure of Crystal Structure of MEK1 Kinase Bound to GDC0973 also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Iodine (I) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of MEK1 Kinase Bound to GDC0973 (pdb code 4lmn). 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 MEK1 Kinase Bound to GDC0973, PDB code: 4lmn:

Magnesium binding site 1 out of 1 in 4lmn

Go back to Magnesium Binding Sites List in 4lmn
Magnesium binding site 1 out of 1 in the Crystal Structure of MEK1 Kinase Bound to GDC0973


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 MEK1 Kinase Bound to GDC0973 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:62.4
occ:1.00
OD2 A:ASP208 2.1 71.2 1.0
OD1 A:ASN195 2.1 75.3 1.0
O2A A:ANP501 2.1 74.6 1.0
O1B A:ANP501 2.1 72.7 1.0
O3G A:ANP501 2.1 64.1 1.0
CG A:ASP208 3.1 66.1 1.0
CG A:ASN195 3.3 76.5 1.0
PA A:ANP501 3.3 70.6 1.0
PB A:ANP501 3.4 69.7 1.0
PG A:ANP501 3.6 69.5 1.0
O3A A:ANP501 3.6 69.6 1.0
O A:SER194 3.7 72.3 1.0
H3' A:ANP501 3.8 80.3 1.0
CB A:ASP208 3.9 60.9 1.0
OD1 A:ASP208 3.9 70.1 1.0
N3B A:ANP501 4.0 68.2 1.0
ND2 A:ASN195 4.1 69.1 1.0
O5' A:ANP501 4.1 69.0 1.0
NZ A:LYS97 4.2 79.5 1.0
OG A:SER194 4.2 64.1 1.0
CB A:ASN195 4.3 57.9 1.0
C A:SER194 4.3 69.0 1.0
CA A:ASN195 4.3 57.9 1.0
O24 A:EUI503 4.3 66.0 1.0
O1A A:ANP501 4.4 72.9 1.0
O1G A:ANP501 4.5 70.9 1.0
N A:ASN195 4.5 60.3 1.0
O2B A:ANP501 4.6 66.1 1.0
O2G A:ANP501 4.7 74.1 1.0
SG A:CYS207 4.9 74.1 1.0
C21 A:EUI503 4.9 66.4 1.0
CE A:LYS97 4.9 65.3 1.0
CB A:SER194 4.9 65.2 1.0
C3' A:ANP501 4.9 80.9 1.0

Reference:

G.Hatzivassiliou, J.R.Haling, H.Chen, K.Song, S.Price, R.Heald, J.F.Hewitt, M.Zak, A.Peck, C.Orr, M.Merchant, K.P.Hoeflich, J.Chan, S.M.Luoh, D.J.Anderson, M.J.Ludlam, C.Wiesmann, M.Ultsch, L.S.Friedman, S.Malek, M.Belvin. Mechanism of Mek Inhibition Determines Efficacy in Mutant Kras- Versus Braf-Driven Cancers. Nature V. 501 232 2013.
ISSN: ISSN 0028-0836
PubMed: 23934108
DOI: 10.1038/NATURE12441
Page generated: Mon Aug 19 19:48:55 2024

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