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Crystal structure of human importin A3 bound to RCC1

Analyse Crystal structure of human importin A3 bound to RCC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TBK
Type
protein
Length
6,677 residues
Chains
16
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Importin subunit alpha-3; Regulator of chromosome condensation
UniProt
O00629, P18754
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 5 distinct chains · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, G, HImportin subunit alpha-3protein41775% helix, 0% strandO00629
B, DImportin subunit alpha-3protein41573% helix, 0% strandO00629
E, FImportin subunit alpha-3protein41673% helix, 0% strandO00629
I, M, PRegulator of chromosome condensationprotein4194% helix, 38% strandP18754
K, L, N, O, JRegulator of chromosome condensationprotein4184% helix, 39% strandP18754

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18170.810.8488empty
28880.800.83102empty
39940.800.81114empty
411060.780.8097empty
510300.770.7997empty

Interfaces

20 interfaces between chains.

  • E–L · 2072 Ų buried · 25 hydrogen bonds · protein-protein
  • A–K · 2067 Ų buried · 35 hydrogen bonds · protein-protein
  • H–O · 2004 Ų buried · 20 hydrogen bonds · protein-protein
  • C–J · 2000 Ų buried · 31 hydrogen bonds · protein-protein
  • D–P · 1962 Ų buried · 37 hydrogen bonds · protein-protein

Compared structures

  • 5TBK · Crystal structure of human importin a3 bound to RCC1 · the same entry in another collection · chain J against J, TM-score 1.00

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