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Crystal structure of the tetratricopeptide repeat (tpr) motif of human dual specificity protein kinase MPS1

Analyse Crystal structure of the tetratricopeptide repeat (tpr) motif of human dual… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H7X
Type: protein
Length: 276 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase ttk
EC: 2.7.12.1
UniProt: P33981
Ligands: PB
Pockets: 4 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dual specificity protein kinase ttk (EC 2.7.12.1)	protein	138	75% helix, 1% strand	P33981

Ligands and binding sites

PB · Lead (II) ion · metal · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.40	0.79	15	empty
2	82	0.36	0.76	21	empty
3	65	0.30	0.75	16	empty
4	65	0.29	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 968 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4H7X · Crystal structure of the tetratricopeptide repeat (TPR) motif of human dual specificity… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P33981
Elsewhere: RCSB PDB 4H7X · PDBe 4H7X · UniProt P33981

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