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Lead in PDB 4h7x: Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1

Enzymatic activity of Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1

All present enzymatic activity of Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1:
2.7.12.1;

Protein crystallography data

The structure of Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1, PDB code: 4h7x was solved by V.M.Bolanos-Garcia, D.Y.Chirgadze, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.70 / 2.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.487, 79.487, 137.684, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24

Lead Binding Sites:

The binding sites of Lead atom in the Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1 (pdb code 4h7x). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1, PDB code: 4h7x:

Lead binding site 1 out of 1 in 4h7x

Go back to Lead Binding Sites List in 4h7x
Lead binding site 1 out of 1 in the Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Crystal Structure of the Tetratricopeptide Repeat (Tpr) Motif of Human Dual Specificity Protein Kinase MPS1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pb201

b:43.3
occ:0.50
 OD1 A:ASP52 3.0 39.2 1.0
OD2 A:ASP52 3.0 48.0 1.0
OE1 B:GLU75 3.0 63.6 1.0
OE2 B:GLU75 3.2 68.8 1.0
CG A:ASP52 3.3 44.8 1.0
CD B:GLU75 3.4 65.6 1.0
OD2 B:ASP78 3.6 44.0 1.0
O B:HOH224 3.7 41.6 1.0
CG B:ASP78 3.7 57.2 1.0
OD1 B:ASP78 3.9 43.2 1.0
CB A:PRO50 4.0 33.6 1.0
CB B:ASP78 4.4 60.3 1.0
CE A:LYS53 4.5 46.5 1.0
NZ A:LYS53 4.7 47.8 1.0
CG A:LYS53 4.7 41.6 1.0
CG A:PRO50 4.8 35.3 1.0
CB A:ASP52 4.8 36.6 1.0
CG B:GLU75 4.9 59.4 1.0

Reference:

P.Thebault, D.Y.Chirgadze, Z.Dou, T.L.Blundell, S.Elowe, V.M.Bolanos-Garcia. Structural and Functional Insights Into the Role of the N-Terminal MPS1 Tpr Domain in the Sac (Spindle Assembly Checkpoint). Biochem.J. V. 448 321 2012.
ISSN: ISSN 0264-6021
PubMed: 23067341
DOI: 10.1042/BJ20121448
Page generated: Thu Oct 10 10:08:28 2024

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