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Cryo-EM (spa) structure of human NUP155 C-terminus (864-1337) at 5.3 ångströms resolution

Analyse Cryo-EM (spa) structure of human NUP155 C-terminus (864-1337) at 5.3 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EYF
Type: protein
Length: 474 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear pore complex protein NUP155
UniProt: O75694
Pockets: 9 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 56% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear pore complex protein NUP155	protein	474	56% helix, 0% strand	O75694

Pockets

9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.81	0.96	23	empty
2	1166	0.81	0.82	109	empty
3	97	0.65	0.90	21	empty
4	167	0.64	0.86	28	empty
5	368	0.64	0.79	31	empty

Compared structures

7EYF · Cryo-EM (SPA) structure of human Nup155 C-terminus (864-1337) at 5.3 Angstroms resolution · the same entry in another collection · chain A against A, TM-score 1.00
O75694 · AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP155 (O75694) · a predicted model of the same protein · chain A against A, TM-score 0.70

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 O75694
Elsewhere: RCSB PDB 7EYF · PDBe 7EYF · UniProt O75694

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