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Crystal structure of the globular region of the prion protein URE2 from yeast saccharomyces cerevisiae

Analyse Crystal structure of the globular region of the prion protein URE2 from yeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G6Y
Type: protein
Length: 502 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: URE2 protein
UniProt: P23202
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	URE2 protein	protein	245	54% helix, 8% strand	P23202
B	URE2 protein	protein	257	60% helix, 7% strand	P23202

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	543	0.73	0.81	39	empty
2	514	0.71	0.80	38	empty
3	206	0.54	0.78	25	empty
4	132	0.42	0.75	27	empty
5	144	0.41	0.74	28	empty

Interfaces

1 interface between chains.

A–B · 1888 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

1G6Y · Crystal structure of the globular region of the prion protein URE2 from yeast… · the same entry in another collection · chain A against A, TM-score 1.00
P23202 · AlphaFold monomer V2.0 prediction for transcriptional regulator URE2 (P23202) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23202
Elsewhere: RCSB PDB 1G6Y · PDBe 1G6Y · UniProt P23202

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