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Crystal structure of the human HIPK3 kinase domain

Analyse Crystal structure of the human HIPK3 kinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7O7I
Type: protein
Length: 367 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homeodomain-interacting protein kinase 3
EC: 2.7.11.1
UniProt: Q9H422
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homeodomain-interacting protein kinase 3 (EC 2.7.11.1)	protein	367	39% helix, 16% strand	Q9H422

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	377	0.65	0.79	39	EDO
2	89	0.39	0.77	17	empty
3	56	0.25	0.72	16	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

7O7I · Crystal structure of the human HIPK3 kinase domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9H422 · AlphaFold monomer V2.0 prediction for homeodomain-interacting protein kinase 3 (Q9H422) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9H422
Elsewhere: RCSB PDB 7O7I · PDBe 7O7I · UniProt Q9H422

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