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Structure of importin A2 bound to P65-nls

Analyse Structure of importin A2 bound to P65-nls in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LEU
Type: protein
Length: 437 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Importin subunit alpha-1; Transcription factor P65
UniProt: P52293, Q04206
Pockets: 1 · best druggability 0.48

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Importin subunit alpha-1	protein	423	74% helix, 0% strand	P52293
B	Transcription factor P65	protein	8	0% helix, 0% strand	Q04206
C	Transcription factor P65	protein	6	0% helix, 0% strand	Q04206

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	69	0.48	0.83	13	empty

Interfaces

2 interfaces between chains.

E–B · 767 Å² buried · 13 hydrogen bonds · protein-protein
E–C · 630 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7LEU · Structure of importin a2 bound to p65-NLS · the same entry in another collection · chain E against E, TM-score 1.00
Q04206 · AlphaFold monomer V2.0 prediction for transcription factor P65 (Q04206) · a predicted model of the same protein · chain C against A, TM-score 0.60

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
Every structure of UniProt Q04206
Elsewhere: RCSB PDB 7LEU · PDBe 7LEU · UniProt P52293 · UniProt Q04206

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