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Crystal structure of hpcna bound to residues 331-350 of the flap endonuclease-1 (FEN1)

Analyse Crystal structure of hpcna bound to residues 331-350 of the flap endonuclease-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U7B
Type
protein
Length
264 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proliferating cell nuclear antigen; Srqgstqgrlddffkvtgsl peptide of flap endonuclease-1
UniProt
P12004, P39748
Pockets
1 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProliferating cell nuclear antigenprotein25119% helix, 47% strandP12004
BSrqgstqgrlddffkvtgsl peptide of flap endonuclease-1protein1323% helix, 15% strandP39748

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1620.400.8012empty

Interfaces

1 interface between chains.

  • A–B · 728 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 1U7B · Crystal structure of hPCNA bound to residues 331-350 of the flap endonuclease-1 (FEN1) · the same entry in another collection · chain A against A, TM-score 1.00
  • P39748 · AlphaFold monomer V2.0 prediction for flap endonuclease 1 (P39748) · a predicted model of the same protein · chain B against A, TM-score 0.33

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