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Crystal structure of a phosphorylated SMAD2

Analyse Crystal structure of a phosphorylated SMAD2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KHX
Type: protein
Length: 203 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SMAD2
UniProt: Q15796
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SMAD2	protein	203	27% helix, 28% strand	Q15796

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.43	0.78	20	empty
2	78	0.33	0.74	13	empty

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

1KHX · Crystal structure of a phosphorylated Smad2 · the same entry in another collection · chain A against A, TM-score 1.00
Q15796 · AlphaFold monomer V2.0 prediction for mothers against decapentaplegic homolog 2 (Q15796) · 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 Q15796
Elsewhere: RCSB PDB 1KHX · PDBe 1KHX · UniProt Q15796

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