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Crystal structure of TGF-beta receptor I kinase with inhibitor

Analyse Crystal structure of TGF-beta receptor I kinase with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PY5
Type: protein
Length: 301 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TGF-beta receptor type I
EC: 2.7.1.37
UniProt: P36897
Ligands: PY1, SO4
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TGF-beta receptor type I (EC 2.7.1.37)	protein	301	39% helix, 19% strand	P36897

Ligands and binding sites

PY1 · 4-(3-pyridin-2-yl-1H-pyrazol-4-yl)quinoline · ligand · chains A
SO4 · Sulfate ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	333	0.73	0.85	43	SO4, PY1
2	108	0.62	0.87	18	empty

Compared structures

1PY5 · Crystal Structure of TGF-beta receptor I kinase with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
P36897 · AlphaFold monomer V2.0 prediction for TGF-beta receptor type-1 (P36897) · 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 P36897
Elsewhere: RCSB PDB 1PY5 · PDBe 1PY5 · UniProt P36897

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