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Crystallization and X-ray diffraction data collection of importin- alpha from mus musculus complexed with a xpg nls peptide, fragment 2

Analyse Crystallization and X-ray diffraction data collection of importin- alpha from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EKG
Type: protein
Length: 439 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: XPG2 peptide; Importin subunit alpha-1
UniProt: P52293
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 3 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	XPG2 peptide	protein	5	0% helix, 0% strand	—
C	XPG2 peptide	protein	9	0% helix, 0% strand	—
A	Importin subunit alpha-1	protein	425	73% helix, 0% strand	P52293

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	0.44	0.81	12	empty

Interfaces

2 interfaces between chains.

C–A · 663 Å² buried · 17 hydrogen bonds · protein-protein
B–A · 551 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5EKG · Crystallization and X-ray Diffraction Data Collection of Importin-alpha from Mus musculus… · 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 5EKG · PDBe 5EKG · UniProt P52293

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