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Structure of LPH2 , a novel bidirectional nuclear transport receptor in S. cerevisiae

Analyse Structure of LPH2 , a novel bidirectional nuclear transport receptor in S.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FVB
Type: protein
Length: 1,001 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Importin beta-like protein KAP120
UniProt: Q02932
Pockets: 14 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Importin beta-like protein KAP120	protein	1001	72% helix, 0% strand	Q02932

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	295	0.62	0.79	41	empty
2	111	0.61	0.86	27	empty
3	241	0.56	0.78	23	empty
4	88	0.43	0.79	19	empty
5	94	0.43	0.78	22	empty

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

6FVB · Structure of Lph2 , a novel bidirectional nuclear transport receptor in S. cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
Q02932 · AlphaFold monomer V2.0 prediction for importin beta-like protein KAP120 (Q02932) · 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 Q02932
Elsewhere: RCSB PDB 6FVB · PDBe 6FVB · UniProt Q02932

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