MolNFT v1 · #177927 · protein

Cryo-EM (spa) structure of human NUP155 longer N-terminus (19-1069) at 5.4 ångström resolution

7EYQ · G PROTEIN/GFP fusion PROTEIN,NUCLEAR pore complex protein…: “Cryo-EM (spa) structure of human NUP155 longer N-terminus (19-1069) at 5.4 ångström resolution”. Electron microscopy, 20 pockets (best druggability 0.86). MolNFT v1…

PDB: 7EYQ
Type: protein
Length: 833 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: G PROTEIN/GFP fusion PROTEIN,NUCLEAR pore complex protein NUP155
UniProt: O75694
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 36% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	G PROTEIN/GFP fusion PROTEIN,NUCLEAR pore complex protein NUP155	protein	833	36% helix, 15% strand	O75694

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1104	0.86	0.87	96	empty
2	900	0.80	0.82	99	empty
3	96	0.72	0.94	30	empty
4	324	0.71	0.84	44	empty
5	290	0.68	0.83	53	empty

Compared structures

7EYQ · Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom… · 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 0.77

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 7EYQ · PDBe 7EYQ · UniProt O75694

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