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Crystal structure of activin receptor type II kinase domain from human

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

PDB: 2QLU
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Activin receptor type iib
EC: 2.7.11.30
UniProt: Q13705
Ligands: ADE, SO4
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Activin receptor type iib (EC 2.7.11.30)	protein	297	39% helix, 20% strand	Q13705

Ligands and binding sites

ADE · Adenine · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · 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	220	0.66	0.84	41	SO4, ADE
2	136	0.49	0.79	20	empty
3	77	0.45	0.82	18	empty

Compared structures

2QLU · Crystal structure of Activin receptor type II kinase domain from human · the same entry in another collection · chain A against A, TM-score 1.00
Q13705 · AlphaFold monomer V2.0 prediction for activin receptor type-2B (Q13705) · 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 Q13705
Elsewhere: RCSB PDB 2QLU · PDBe 2QLU · UniProt Q13705

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