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Zinc in PDB 2ac3: Structure of Human MNK2 Kinase Domain

Enzymatic activity of Structure of Human MNK2 Kinase Domain

All present enzymatic activity of Structure of Human MNK2 Kinase Domain:
2.7.1.37;

Protein crystallography data

The structure of Structure of Human MNK2 Kinase Domain, PDB code: 2ac3 was solved by R.Jauch, M.C.Wahl, C.Netter, S.Jakel, K.Schreiter, B.Aicher, H.Jackle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.10
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 104.502, 104.502, 72.351, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human MNK2 Kinase Domain (pdb code 2ac3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Human MNK2 Kinase Domain, PDB code: 2ac3:

Zinc binding site 1 out of 1 in 2ac3

Go back to Zinc Binding Sites List in 2ac3
Zinc binding site 1 out of 1 in the Structure of Human MNK2 Kinase Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human MNK2 Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn531

b:90.3
occ:1.00
SG A:CYS311 2.3 86.5 1.0
SG A:CYS299 2.3 92.1 1.0
CB A:CYS303 2.4 0.8 1.0
SG A:CYS314 2.5 75.4 1.0
SG A:CYS303 2.5 99.4 1.0
CB A:CYS311 3.2 86.2 1.0
CB A:CYS314 3.4 74.1 1.0
CB A:CYS299 3.8 90.8 1.0
N A:CYS314 3.8 73.2 1.0
CA A:CYS303 3.9 96.6 1.0
CA A:CYS314 4.1 71.4 1.0
N A:CYS299 4.5 81.5 1.0
N A:CYS303 4.6 0.4 1.0
CA A:CYS311 4.6 83.7 1.0
NE1 A:TRP305 4.7 0.2 1.0
CB A:ALA313 4.7 74.0 1.0
C A:CYS303 4.8 95.6 1.0
CD1 A:TRP305 4.8 0.7 1.0
CA A:CYS299 4.8 89.3 1.0
C A:ALA313 4.8 75.2 1.0
N A:GLY304 4.9 94.6 1.0

Reference:

R.Jauch, S.Jakel, C.Netter, K.Schreiter, B.Aicher, H.Jackle, M.C.Wahl. Crystal Structures of the MNK2 Kinase Domain Reveal An Inhibitory Conformation and A Zinc Binding Site. Structure V. 13 1559 2005.
ISSN: ISSN 0969-2126
PubMed: 16216586
DOI: 10.1016/J.STR.2005.07.013
Page generated: Wed Dec 16 03:17:12 2020

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