MolNFT v1 · #2041 · protein

Karyopherin alpha from saccharomyces cerevisiae

1BK5: “Karyopherin alpha from saccharomyces cerevisiae”. X-ray diffraction, 1 ligand (CO), 2 pockets (best druggability 0.75). MolNFT v1 #2041 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1BK5
Type: protein
Length: 844 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Karyopherin alpha
UniProt: Q02821
Ligands: CO
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Karyopherin alpha	protein	422	75% helix, 0% strand	Q02821

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	751	0.75	0.80	78	CO
2	696	0.73	0.79	75	CO

Interfaces

1 interface between chains.

A–B · 1216 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1BK5 · Karyopherin alpha from saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
Q02821 · AlphaFold monomer V2.0 prediction for importin subunit alpha (Q02821) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q02821
Elsewhere: RCSB PDB 1BK5 · PDBe 1BK5 · UniProt Q02821

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