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Crystal structure of human interleukin-19

Analyse Crystal structure of human interleukin-19 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1N1F
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interleukin-19
UniProt: Q9UHD0
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interleukin-19	protein	153	70% helix, 1% strand	Q9UHD0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

1N1F · Crystal Structure of Human Interleukin-19 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UHD0 · AlphaFold monomer V2.0 prediction for interleukin-19 (Q9UHD0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9UHD0
Elsewhere: RCSB PDB 1N1F · PDBe 1N1F · UniProt Q9UHD0

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