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Magnesium in PDB 3alo: Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide

Enzymatic activity of Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide

All present enzymatic activity of Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide:
2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide, PDB code: 3alo was solved by T.Matsumoto, T.Kinoshita, Y.Kirii, K.Yokota, K.Hamada, T.Tada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 68.776, 117.985, 81.793, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide (pdb code 3alo). 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 Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide, PDB code: 3alo:

Magnesium binding site 1 out of 1 in 3alo

Go back to Magnesium Binding Sites List in 3alo
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 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 Human Non-Phosphorylated MKK4 Kinase Domain Ternary Complex with Amp-Pnp and P38 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:32.0
occ:1.00
 O1A A:ANP406 1.9 36.1 1.0
O2B A:ANP406 2.0 27.5 1.0
OD2 A:ASP247 2.1 29.2 1.0
OD1 A:ASN234 2.2 27.4 1.0
O3G A:ANP406 2.2 28.6 1.0
PA A:ANP406 3.2 29.5 1.0
PB A:ANP406 3.2 33.4 1.0
CG A:ASP247 3.3 31.4 1.0
CG A:ASN234 3.3 24.7 1.0
C5' A:ANP406 3.3 57.1 1.0
PG A:ANP406 3.4 33.0 1.0
O3A A:ANP406 3.5 34.2 1.0
NZ A:LYS131 3.7 29.3 1.0
N3B A:ANP406 3.8 28.8 1.0
O5' A:ANP406 3.8 37.0 1.0
O A:SER233 3.8 30.2 1.0
ND2 A:ASN234 3.9 25.3 1.0
CB A:ASP247 4.1 31.3 1.0
O2G A:ANP406 4.2 30.8 1.0
OD1 A:ASP247 4.2 36.3 1.0
OG A:SER233 4.2 30.9 1.0
SG A:CYS246 4.3 30.2 1.0
O2A A:ANP406 4.4 31.2 1.0
C A:SER233 4.5 25.4 1.0
O1B A:ANP406 4.5 32.5 1.0
CB A:ASN234 4.5 23.9 1.0
CA A:ASN234 4.6 23.6 1.0
O1G A:ANP406 4.6 32.6 1.0
C4' A:ANP406 4.7 48.6 1.0
C8 A:ANP406 4.7 28.9 1.0
N A:ASN234 4.8 25.3 1.0

Reference:

T.Matsumoto, T.Kinoshita, Y.Kirii, K.Yokota, K.Hamada, T.Tada. Crystal Structures of MKK4 Kinase Domain Reveal That Substrate Peptide Binds to An Allosteric Site and Induces An Auto-Inhibition State Biochem.Biophys.Res.Commun. V. 400 369 2010.
ISSN: ISSN 0006-291X
PubMed: 20732303
DOI: 10.1016/J.BBRC.2010.08.071
Page generated: Wed Aug 14 08:42:09 2024

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