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Zinc in PDB 5twh: Human MOB1A Bound to MST1 Phosphorylated T367 Peptide

Protein crystallography data

The structure of Human MOB1A Bound to MST1 Phosphorylated T367 Peptide, PDB code: 5twh was solved by S.Xiong, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.00 / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.986, 60.986, 138.486, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 26

Zinc Binding Sites:

The binding sites of Zinc atom in the Human MOB1A Bound to MST1 Phosphorylated T367 Peptide (pdb code 5twh). 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 Human MOB1A Bound to MST1 Phosphorylated T367 Peptide, PDB code: 5twh:

Zinc binding site 1 out of 1 in 5twh

Go back to Zinc Binding Sites List in 5twh
Zinc binding site 1 out of 1 in the Human MOB1A Bound to MST1 Phosphorylated T367 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human MOB1A Bound to MST1 Phosphorylated T367 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:73.3
occ:1.00
NE2 A:HIS161 2.0 0.1 1.0
NE2 A:HIS166 2.1 57.2 1.0
SG A:CYS84 2.4 82.7 1.0
SG A:CYS79 2.4 63.3 1.0
CD2 A:HIS166 2.8 62.3 1.0
CE1 A:HIS161 2.8 0.5 1.0
CD2 A:HIS161 3.1 0.3 1.0
CB A:CYS79 3.2 60.4 1.0
CE1 A:HIS166 3.3 61.4 1.0
CB A:CYS84 3.4 88.6 1.0
CA A:CYS79 3.8 62.4 1.0
ND1 A:HIS161 4.0 0.8 1.0
CG A:HIS166 4.1 62.9 1.0
CG A:HIS161 4.2 0.1 1.0
CB A:ALA111 4.2 60.7 1.0
ND1 A:HIS166 4.3 63.8 1.0
CB A:GLN165 4.5 66.0 1.0
C A:CYS79 4.7 66.9 1.0
CG A:GLN165 4.8 72.6 1.0
N A:CYS79 4.8 61.7 1.0
CA A:CYS84 4.9 91.0 1.0
N A:THR80 5.0 66.5 1.0

Reference:

A.L.Couzens, S.Xiong, J.D.R.Knight, D.Y.Mao, S.Guettler, S.Picaud, I.Kurinov, P.Filippakopoulos, F.Sicheri, A.C.Gingras. MOB1 Mediated Phospho-Recognition in the Core Mammalian Hippo Pathway. Mol. Cell Proteomics V. 16 1098 2017.
ISSN: ESSN 1535-9484
PubMed: 28373298
DOI: 10.1074/MCP.M116.065490
Page generated: Mon Oct 28 08:56:30 2024

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