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The JAK1 kinase domain in complex with compound 37

Analyse The JAK1 kinase domain in complex with compound 37 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K6Z
Type: protein
Length: 281 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase JAK1
EC: 2.7.10.2
UniProt: P23458
Ligands: 1Q3
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase JAK1 (EC 2.7.10.2)	protein	281	39% helix, 21% strand	P23458

Ligands and binding sites

1Q3 · (1R,2S)-2-{[8-oxo-2-(1H-pyrazol-4-yl)-5,8-dihydropyrido[3,4-d]pyrimidin-4-yl]amino}cyclopentanecarbonitrile · ligand · chains A

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

Pockets

2 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	295	0.72	0.86	51	1Q3
2	93	0.35	0.74	20	empty

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

4K6Z · The Jak1 kinase domain in complex with compound 37 · 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 P23458
Elsewhere: RCSB PDB 4K6Z · PDBe 4K6Z · UniProt P23458

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