GL1X · GenesisL1 explorer

MolNFT v1 · #118212 · protein + DNA

Structure II of intact U2AF65 recognizing the 3' splice site signal

5EV2 · Splicing factor U2AF 65 kda subunit: “Structure II of intact U2AF65 recognizing the 3' splice site signal”. X-ray diffraction, 1 pocket (best druggability 0.28). MolNFT v1 #118212 on GenesisL1: 3D structure, binding sites and…

PDB
5EV2
Type
protein + DNA
Length
206 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Splicing factor U2AF 65 kda subunit; DNA (5'-R(P*UP*U)-D(P*UP*U)-R(P*U)-D(P*UP*(BRU)P*U)-3…
UniProt
P26368
Pockets
1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASplicing factor U2AF 65 kda subunitprotein19827% helix, 29% strandP26368
BDNA (5'-R(P*UP*U)-D(P*UP*U)-R(P*U)-D(P*UP*(BRU)P*U)-3')dna8——

Ligands and binding sites

  • DIO · 1,4-diethylene dioxide · additive · chains A
  • PGE · Triethylene glycol · additive · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A

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
1670.280.7317empty

Interfaces

1 interface between chains.

  • A–B · 1240 Ų buried · 36 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 1 modified (nucleotide modification).

Compared structures

  • 5EV2 · Structure II of Intact U2AF65 Recognizing the 3' Splice Site Signal · the same entry in another collection · chain A against A, TM-score 1.00
  • P26368 · AlphaFold monomer V2.0 prediction for splicing factor U2AF 65 kda subunit (P26368) · a predicted model of the same protein · chain A against A, TM-score 0.82

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.