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MolNFT v1 · #38938 · protein

Structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein

2HE9 · Nk-tumor recognition protein: “Structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.29). MolNFT v1 #38938 on GenesisL1: 3D…

PDB
2HE9
Type
protein
Length
344 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nk-tumor recognition protein
EC
5.2.1.8
UniProt
P30414
Ligands
SO4
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNk-tumor recognition protein (EC 5.2.1.8)protein17213% helix, 33% strandP30414

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A, 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.290.7415empty

Interfaces

1 interface between chains.

  • A–B · 564 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2HE9 · Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition… · the same entry in another collection · chain A against A, TM-score 1.00
  • P30414 · AlphaFold monomer V2.0 prediction for nk-tumor recognition protein (P30414) · a predicted model of the same protein · chain A against A, TM-score 0.99

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