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Human alpha-defensin 1 derivative (HNP1)

Analyse Human alpha-defensin 1 derivative (HNP1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2PM5
Type
protein
Length
60 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Neutrophil defensin 1 (hnp-1) (hp-1) (HP1) (defensin, alpha 1)
UniProt
P59665
Ligands
PO4

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNeutrophil defensin 1 (hnp-1) (hp-1) (HP1) (defensin, alpha 1)protein300% helix, 53% strandP59665

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 114 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 6 modified (disulfide, nonstandard).

Compared structures

  • 2PM5 · Human alpha-defensin 1 derivative (HNP1) · the same entry in another collection · chain A against A, TM-score 1.00
  • P59665 · AlphaFold monomer V2.0 prediction for neutrophil defensin 1 (P59665) · a predicted model of the same protein · chain B against A, TM-score 0.82

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