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NMR structure of rrm-2 of yeast NPL3 protein

Analyse NMR structure of rrm-2 of yeast NPL3 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OSR
Type: protein
Length: 87 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleolar protein 3
UniProt: Q01560
Pockets: 1 · best druggability 0.60

Structure

solution nmr · 1 distinct chain · 24% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleolar protein 3	protein	87	24% helix, 25% strand	Q01560

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.60	0.86	22	empty

Compared structures

2OSR · NMR Structure of RRM-2 of Yeast NPL3 Protein · the same entry in another collection · chain A against A, TM-score 1.00
Q01560 · AlphaFold monomer V2.0 prediction for nucleolar protein 3 (Q01560) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 Q01560
Elsewhere: RCSB PDB 2OSR · PDBe 2OSR · UniProt Q01560

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