Research workbench

Cryoem structure of human NUP155 (residues 19-981)

Analyse Cryoem structure of human NUP155 (residues 19-981) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7R1Y
Type: protein
Length: 723 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear pore complex protein NUP155
UniProt: O75694
Pockets: 7 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear pore complex protein NUP155	protein	723	38% helix, 22% strand	O75694

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1032	0.76	0.78	57	empty
2	115	0.65	0.89	26	empty
3	95	0.56	0.86	26	empty
4	94	0.52	0.84	17	empty
5	141	0.47	0.78	20	empty

Compared structures

7R1Y · cryoEM structure of human Nup155 (residues 19-981) · 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 0.95

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 7R1Y · PDBe 7R1Y · UniProt O75694

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