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Crystal structure of chaetomium thermophilum NUP192

Analyse Crystal structure of chaetomium thermophilum NUP192 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HB4
Type: protein
Length: 1,388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NUP192,NUCLEOPORIN NUP192
UniProt: G0S4T0
Ligands: OS
Pockets: 20 · best druggability 0.68

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	NUP192,NUCLEOPORIN NUP192	protein	1388	66% helix, 1% strand	G0S4T0

Ligands and binding sites

OS · Osmium ion · metal · 5 copies · chains B

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	623	0.68	0.77	61	empty
2	154	0.60	0.84	26	empty
3	251	0.59	0.79	40	empty
4	163	0.57	0.81	31	empty
5	304	0.56	0.76	41	empty

Compared structures

5HB4 · Crystal structure of Chaetomium thermophilum Nup192 · the same entry in another collection · chain B against B, TM-score 1.00
G0S4T0 · AlphaFold monomer V2.0 prediction for nucleoporin NUP192 (G0S4T0) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 G0S4T0
Elsewhere: RCSB PDB 5HB4 · PDBe 5HB4 · UniProt G0S4T0

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