Research workbench

Karyopherin BETA2/TRANSPORTIN

Analyse Karyopherin BETA2/TRANSPORTIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QMR
Type: protein
Length: 3,295 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transportin-1
UniProt: Q92973
Pockets: 20 · best druggability 0.59

Structure

x-ray diffraction · 4 distinct chains · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transportin-1	protein	835	76% helix, 0% strand	Q92973
B	Transportin-1	protein	801	76% helix, 0% strand	Q92973
C	Transportin-1	protein	824	76% helix, 0% strand	Q92973
D	Transportin-1	protein	835	76% helix, 0% strand	Q92973

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	286	0.59	0.78	34	empty
2	337	0.59	0.76	39	empty
3	370	0.58	0.75	48	empty
4	70	0.56	0.88	21	empty
5	148	0.54	0.81	24	empty

Interfaces

4 interfaces between chains.

B–D · 577 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 536 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 433 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 378 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2QMR · Karyopherin beta2/transportin · the same entry in another collection · chain C against C, TM-score 1.00
Q92973 · AlphaFold monomer V2.0 prediction for transportin-1 (Q92973) · a predicted model of the same protein · chain C against A, TM-score 0.90

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 Q92973
Elsewhere: RCSB PDB 2QMR · PDBe 2QMR · UniProt Q92973

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