Research workbench

Crystal structure of novel tudor domain-containing protein SGF29

Analyse Crystal structure of novel tudor domain-containing protein SGF29 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MEW
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saga-associated factor 29 homolog
UniProt: Q96ES7
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saga-associated factor 29 homolog	protein	157	6% helix, 43% strand	Q96ES7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.44	0.78	24	empty

Compared structures

3MEW · Crystal structure of Novel Tudor domain-containing protein SGF29 · the same entry in another collection · chain A against A, TM-score 1.00
Q96ES7 · AlphaFold monomer V2.0 prediction for saga-associated factor 29 (Q96ES7) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q96ES7
Elsewhere: RCSB PDB 3MEW · PDBe 3MEW · UniProt Q96ES7

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