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Importin binding to tdt nls peptide

Analyse Importin binding to tdt nls peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W4E
Type: protein
Length: 438 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Importin subunit alpha-1,IMPORTIN subunit alpha-1; Human DNA repair polymerase tdt
UniProt: P52293
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 3 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Importin subunit alpha-1,IMPORTIN subunit alpha-1	protein	425	74% helix, 0% strand	P52293
A	Human DNA repair polymerase tdt	protein	10	0% helix, 0% strand	—
D	Human DNA repair polymerase tdt	protein	3	0% helix, 0% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.42	0.80	13	GOL

Interfaces

2 interfaces between chains.

B–A · 781 Å² buried · 19 hydrogen bonds · protein-protein
B–D · 299 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5W4E · Importin binding to Tdt NLS peptide · the same entry in another collection · chain B against B, TM-score 1.00

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 P52293
Elsewhere: RCSB PDB 5W4E · PDBe 5W4E · UniProt P52293

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