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Human beta-defensin-1 (mutant GLN11ALA)

Analyse Human beta-defensin-1 (mutant GLN11ALA) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NLE
Type
protein
Length
72 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-defensin 1
UniProt
P60022
Ligands
SO4

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta-defensin 1protein3617% helix, 33% strandP60022

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • ACT · Acetate ion · additive · chains A

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

Interfaces

1 interface between chains.

  • A–B · 42 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 2NLE · Human beta-defensin-1 (Mutant Gln11Ala) · the same entry in another collection · chain A against A, TM-score 1.00
  • P60022 · AlphaFold monomer V2.0 prediction for beta-defensin 1 (P60022) · a predicted model of the same protein · chain A against A, TM-score 0.87

Analyse

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