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X-ray structure of the RNA-binding protein SHE2P

Analyse X-ray structure of the RNA-binding protein SHE2P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XLY
Type: protein
Length: 408 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SHE2P
UniProt: P36068
Pockets: 5 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SHE2P	protein	224	75% helix, 1% strand	P36068
B	SHE2P	protein	184	83% helix, 0% strand	P36068

Pockets

5 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	99	0.56	0.85	20	empty
2	84	0.52	0.84	20	empty
3	61	0.45	0.83	17	empty
4	97	0.34	0.73	17	empty
5	91	0.34	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 2107 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

1XLY · X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p · the same entry in another collection · chain A against A, TM-score 1.00
P36068 · AlphaFold monomer V2.0 prediction for SWI5-dependent ho expression protein 2 (P36068) · 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 P36068
Elsewhere: RCSB PDB 1XLY · PDBe 1XLY · UniProt P36068

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