Zinc in PDB 4il3: Crystal Structure of S. Mikatae STE24P

All present enzymatic activity of Crystal Structure of S. Mikatae STE24P:
3.4.24.84;

The structure of Crystal Structure of S. Mikatae STE24P, PDB code: 4il3 was solved by E.E.Pryor Jr., P.S.Horanyi, K.Clark, N.Fedoriw, S.M.Connelly, M.Koszelak-Rosenblum, G.Zhu, M.G.Malkowski, M.E.Dumont, M.C.Wiener, Membrane Proteinstructural Biology Consortium (Mpsbc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.45 / 3.10
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	143.530, 143.530, 197.024, 90.00, 90.00, 120.00
R / Rfree (%)	27 / 29.3

The binding sites of Zinc atom in the Crystal Structure of S. Mikatae STE24P (pdb code 4il3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of S. Mikatae STE24P, PDB code: 4il3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of S. Mikatae STE24P


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 S. Mikatae STE24P within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:74.9 occ:1.00 OE1 A:GLU390 2.0 79.8 1.0 OE2 A:GLU390 2.0 79.2 1.0 NE2 A:HIS301 2.0 59.4 1.0 NE2 A:HIS297 2.1 72.4 1.0 CD A:GLU390 2.3 79.8 1.0 CE1 A:HIS301 2.6 60.6 1.0 CD2 A:HIS297 2.9 73.5 1.0 CE1 A:HIS297 3.1 72.1 1.0 CD2 A:HIS301 3.3 59.3 1.0 CG A:GLU390 3.8 80.5 1.0 ND1 A:HIS301 3.9 61.8 1.0 OE1 A:GLU298 3.9 78.0 1.0 CG A:HIS297 4.0 74.0 1.0 ND1 A:HIS297 4.1 73.1 1.0 NE2 A:HIS434 4.2 59.7 1.0 CG A:HIS301 4.2 60.5 1.0 CD2 A:HIS434 4.5 60.6 1.0 CB A:GLU390 4.6 80.9 1.0 CA A:GLU390 4.7 59.6 1.0 NH2 A:ARG440 4.7 60.9 1.0 O A:HIS297 4.8 0.5 1.0 CD A:GLU298 5.0 77.2 1.0 CB A:ALA393 5.0 82.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of S. Mikatae STE24P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of S. Mikatae STE24P within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:65.2 occ:1.00 OE1 B:GLU390 2.0 90.7 1.0 OE2 B:GLU390 2.0 90.0 1.0 CE1 B:HIS301 2.0 91.3 1.0 NE2 B:HIS297 2.1 89.3 1.0 NE2 B:HIS301 2.1 90.8 1.0 CD B:GLU390 2.3 90.6 1.0 CD2 B:HIS297 3.0 86.3 1.0 CE1 B:HIS297 3.0 90.6 1.0 ND1 B:HIS301 3.4 90.7 1.0 CD2 B:HIS301 3.4 89.7 1.0 OE2 B:GLU298 3.7 86.3 1.0 CG B:GLU390 3.8 91.7 1.0 CG B:HIS301 4.0 89.6 1.0 ND1 B:HIS297 4.0 88.4 1.0 CG B:HIS297 4.1 85.8 1.0 CB B:GLU390 4.6 92.5 1.0 CD B:GLU298 4.6 84.5 1.0 CA B:GLU390 4.7 55.8 1.0 CB B:ALA393 4.8 52.2 1.0 O B:HIS297 4.9 83.2 1.0

E.E.Pryor, P.S.Horanyi, K.M.Clark, N.Fedoriw, S.M.Connelly, M.Koszelak-Rosenblum, G.Zhu, M.G.Malkowski, M.C.Wiener, M.E.Dumont. Structure of the Integral Membrane Protein Caax Protease STE24P. Science V. 339 1600 2013.
ISSN: ISSN 0036-8075
PubMed: 23539602
DOI: 10.1126/SCIENCE.1232048