Research workbench

RIMP_ALPHA_B54NLS

Analyse RIMP_ALPHA_B54NLS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YNS
Type: protein
Length: 862 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Importin subunit alpha-1A; B54NLS
UniProt: Q71VM4
Pockets: 3 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Importin subunit alpha-1A	protein	422	74% helix, 0% strand	Q71VM4
C, D	B54NLS	protein	9	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.29	0.75	9	empty
2	54	0.28	0.74	11	empty
3	52	0.28	0.74	11	empty

Interfaces

2 interfaces between chains.

A–C · 793 Å² buried · 25 hydrogen bonds · protein-protein
B–D · 784 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

2YNS · rImp_alpha_B54NLS · the same entry in another collection · chain A against A, TM-score 1.00
Q71VM4 · AlphaFold monomer V2.0 prediction for importin subunit alpha-1A (Q71VM4) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q71VM4
Elsewhere: RCSB PDB 2YNS · PDBe 2YNS · UniProt Q71VM4

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