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Structure of pross-edited human interleukin 24

Analyse Structure of pross-edited human interleukin 24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GG1
Type: protein
Length: 145 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q13007
Ligands: NI, SO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	145	—	Q13007

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Compared structures

6GG1 · Structure of PROSS-edited human interleukin 24 · the same entry in another collection · chain A against A, TM-score 1.00
Q13007 · AlphaFold monomer V2.0 prediction for interleukin-24 (Q13007) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q13007
Elsewhere: RCSB PDB 6GG1 · PDBe 6GG1 · UniProt Q13007

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