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Zinc in PDB 2hw7: Crystal Structure of MNK2-D228G in Complex with Staurosporine

Enzymatic activity of Crystal Structure of MNK2-D228G in Complex with Staurosporine

All present enzymatic activity of Crystal Structure of MNK2-D228G in Complex with Staurosporine:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of MNK2-D228G in Complex with Staurosporine, PDB code: 2hw7 was solved by R.Jauch, M.C.Wahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.71
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 102.366, 102.366, 76.439, 90.00, 90.00, 120.00
R / Rfree (%) 20.1 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of MNK2-D228G in Complex with Staurosporine (pdb code 2hw7). 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 Crystal Structure of MNK2-D228G in Complex with Staurosporine, PDB code: 2hw7:

Zinc binding site 1 out of 1 in 2hw7

Go back to Zinc Binding Sites List in 2hw7
Zinc binding site 1 out of 1 in the Crystal Structure of MNK2-D228G in Complex with Staurosporine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of MNK2-D228G in Complex with Staurosporine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn41

b:84.5
occ:1.00
SG A:CYS311 1.8 95.0 1.0
SG A:CYS314 1.9 95.4 1.0
SG A:CYS299 2.4 85.0 1.0
CB A:CYS311 3.1 95.4 1.0
CB A:CYS314 3.6 93.0 1.0
N A:CYS314 4.0 93.2 1.0
CB A:CYS299 4.2 82.9 1.0
CA A:CYS314 4.2 92.8 1.0
CB A:ALA313 4.3 93.8 1.0
CA A:CYS311 4.4 95.4 1.0
SG A:CYS303 4.5 0.3 1.0
O A:CYS311 4.7 95.6 1.0
C A:CYS311 4.7 95.5 1.0
N A:CYS299 4.9 82.0 1.0
C A:ALA313 4.9 93.6 1.0

Reference:

R.Jauch, M.K.Cho, C.Netter, K.Schreiter, B.Aicher, M.Zweckstetter, M.C.Wahl. Mitogen-Activated Protein Kinases Interacting Kinases Are Autoinhibited By A Reprogrammed Activation Segment. Embo J. V. 25 4020 2006.
ISSN: ISSN 0261-4189
PubMed: 16917500
DOI: 10.1038/SJ.EMBOJ.7601285
Page generated: Wed Dec 16 03:30:29 2020

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