Research workbench

Human IFNAR1

Analyse Human IFNAR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S98
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon ALPHA/BETA receptor 1
UniProt: P17181
Ligands: NAG
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interferon ALPHA/BETA receptor 1	protein	270	6% helix, 48% strand	P17181

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.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	213	0.47	0.74	30	empty
2	105	0.45	0.78	19	empty
3	92	0.41	0.77	19	empty

Modifications

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

Compared structures

3S98 · human IFNAR1 · the same entry in another collection · chain A against A, TM-score 1.00
P17181 · AlphaFold monomer V2.0 prediction for interferon ALPHA/BETA receptor 1 (P17181) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P17181
Elsewhere: RCSB PDB 3S98 · PDBe 3S98 · UniProt P17181

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