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Crystal structure of covalent dimer of HNP1

Analyse Crystal structure of covalent dimer of HNP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HJ2
Type: protein
Length: 66 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human neutrophil peptide 1
UniProt: P59665

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Human neutrophil peptide 1	protein	33	0% helix, 52% strand	P59665

Interfaces

1 interface between chains.

A–B · 581 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

3HJ2 · Crystal structure of covalent dimer of HNP1 · the same entry in another collection · chain B against B, TM-score 1.00
P59665 · AlphaFold monomer V2.0 prediction for neutrophil defensin 1 (P59665) · a predicted model of the same protein · chain A against A, TM-score 0.78

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P59665
Elsewhere: RCSB PDB 3HJ2 · PDBe 3HJ2 · UniProt P59665

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