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Human protein kinase C theta in complex with COMPOUND35 ((1R)-9- (azetidin-3-ylamino)-1,8-dimethyl-3,5-DIHYDRO[1,2,4]TRIAZINO[3,4- C][1,4]BENZOXAZIN-2(1H)-one)

Analyse Human protein kinase C theta in complex with COMPOUND35 ((1R)-9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q9Z
Type: protein
Length: 642 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human protein kinase C theta
EC: 2.7.11.13
UniProt: Q04759
Ligands: PZW, NA
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human protein kinase C theta (EC 2.7.11.13)	protein	333	40% helix, 17% strand	Q04759
B	Human protein kinase C theta (EC 2.7.11.13)	protein	309	38% helix, 18% strand	Q04759

Ligands and binding sites

PZW · (1R)-9-(azetidin-3-ylamino)-1,8-dimethyl-3,5-dihydro[1,2,4]triazino[3,4-c][1,4]benzoxazin-2(1H)-one · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	659	0.77	0.83	64	PZW
2	532	0.72	0.81	58	PZW
3	258	0.56	0.77	27	empty
4	81	0.34	0.74	15	empty
5	70	0.29	0.73	19	empty

Interfaces

1 interface between chains.

A–B · 846 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (phosphorylation).

Compared structures

4Q9Z · Human Protein Kinase C Theta in Complex with Compound35… · the same entry in another collection · chain A against A, TM-score 1.00
Q04759 · AlphaFold monomer V2.0 prediction for protein kinase C theta type (Q04759) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q04759
Elsewhere: RCSB PDB 4Q9Z · PDBe 4Q9Z · UniProt Q04759

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