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Ribosome assembly factor NSA1: C-terminal truncation

Analyse Ribosome assembly factor NSA1: C-terminal truncation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5SUI
Type: protein
Length: 382 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosome biogenesis protein NSA1
UniProt: P53136
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribosome biogenesis protein NSA1	protein	382	3% helix, 49% strand	P53136

Pockets

2 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	820	0.78	0.82	78	empty
2	117	0.52	0.81	26	empty

Compared structures

5SUI · Ribosome assembly factor NSA1: C-terminal truncation · the same entry in another collection · chain A against A, TM-score 1.00
P53136 · AlphaFold monomer V2.0 prediction for ribosome biogenesis protein NSA1 (P53136) · 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 P53136
Elsewhere: RCSB PDB 5SUI · PDBe 5SUI · UniProt P53136

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