Research workbench

Crystal structure of chaetomium thermophilum NUP188 tail domain

Analyse Crystal structure of chaetomium thermophilum NUP188 tail domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CWU
Type: protein
Length: 2,384 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoporin NUP188
UniProt: G0SFH5
Pockets: 20 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Nucleoporin NUP188	protein	298	66% helix, 0% strand	G0SFH5

Ligands and binding sites

GOL · Glycerol · additive · 8 copies · chains A, H, B, C, G, D, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.72	0.89	40	GOL
2	341	0.72	0.84	58	GOL
3	142	0.72	0.90	21	empty
4	172	0.71	0.89	25	empty
5	160	0.70	0.89	24	empty

Interfaces

10 interfaces between chains.

C–H · 786 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 784 Å² buried · 8 hydrogen bonds · protein-protein
A–H · 596 Å² buried · 4 hydrogen bonds · protein-protein
C–G · 572 Å² buried · 5 hydrogen bonds · protein-protein
D–E · 210 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

5CWU · Crystal structure of Chaetomium thermophilum Nup188 TAIL domain · the same entry in another collection · chain H against H, TM-score 1.00
G0SFH5 · AlphaFold monomer V2.0 prediction for nucleoporin NUP188 (G0SFH5) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 G0SFH5
Elsewhere: RCSB PDB 5CWU · PDBe 5CWU · UniProt G0SFH5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.