A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site. Determined by solution NMR. Released 5 Dec 2012.
Explore 2LMS in 3D Show helices and sheets RCSB PDB PDBe
2LMS contains 8 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-21 | 12 | |
| α-helix | 26-28 | 3 | |
| α-helix | 40-43 | 4 | |
| α-helix | 52-67 | 16 | |
| α-helix | 70-75 | 6 | |
| α-helix | 78-100 | 23 | |
| α-helix | 109-132 | 24 | |
| α-helix | 139-155 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interferon alpha-2 | A | protein | 166 | Homo sapiens | P01563 (AlphaFold model) |
>2LMS_1 Interferon alpha-2 (chains A) MCDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A2G | 2-acetamido-2-deoxy-alpha-D-galactopyranose | C8 H15 N O6 | 1 |
A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site. Ghasriani, H., Belcourt, P.J., Sauve, S. et al. J Biol Chem (2013) 288:247-254. DOI 10.1074/jbc.M112.413252 · PubMed
Other PDB entries of the same protein (UniProt P01563 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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