Crystal structure of human glycogenin-2 catalytic domain. Determined by X-ray diffraction at 1.93 Å resolution. Released 24 Dec 2014.
Explore 4UEG in 3D Show helices and sheets RCSB PDB PDBe
4UEG contains 37 α-helices and 20 β-strands across 2 chains. 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 |
|---|---|---|---|
| β-strand | 6-12 | 7 | 1 |
| α-helix | 18-30 | 13 | |
| β-strand | 36-41 | 6 | 1 |
| α-helix | 47-53 | 7 | |
| β-strand | 59-62 | 4 | 1 |
| α-helix | 70-78 | 9 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-89 | 7 | |
| α-helix | 90-93 | 4 | |
| β-strand | 99-103 | 5 | 1 |
| β-strand | 107-109 | 3 | 2 |
| α-helix | 114-118 | 5 | |
| α-helix | 120 | 1 | |
| β-strand | 123-126 | 4 | 1 |
| α-helix | 127 | 1 | |
| β-strand | 134-141 | 8 | 1 |
| α-helix | 145-158 | 14 | |
| α-helix | 165-172 | 8 | |
| α-helix | 181-183 | 3 | |
| β-strand | 184 | 1 | 1 |
| α-helix | 187-189 | 3 | |
| β-strand | 191 | 1 | 2 |
| α-helix | 201-206 | 6 | |
| α-helix | 207-209 | 3 | |
| β-strand | 212-214 | 3 | 2 |
| α-helix | 221-223 | 3 | |
| α-helix | 246-255 | 10 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-267 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-12 | 7 | 3 |
| α-helix | 18-30 | 13 | |
| β-strand | 36-41 | 6 | 3 |
| α-helix | 47-53 | 7 | |
| β-strand | 59-62 | 4 | 3 |
| α-helix | 70-78 | 9 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-89 | 7 | |
| α-helix | 90-93 | 4 | |
| β-strand | 99-103 | 5 | 3 |
| β-strand | 107-109 | 3 | 4 |
| α-helix | 114-118 | 5 | |
| β-strand | 123-126 | 4 | 3 |
| α-helix | 127 | 1 | |
| β-strand | 134-141 | 8 | 3 |
| α-helix | 145-158 | 14 | |
| α-helix | 165-172 | 8 | |
| α-helix | 181-183 | 3 | |
| β-strand | 184 | 1 | 3 |
| α-helix | 187-189 | 3 | |
| β-strand | 191-192 | 2 | 4 |
| α-helix | 201-206 | 6 | |
| α-helix | 207-209 | 3 | |
| β-strand | 212-214 | 3 | 4 |
| α-helix | 221-224 | 4 | |
| α-helix | 243-255 | 13 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-264 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogenin-2 | A, B | protein | 288 | HOMO SAPIENS | O15488 (AlphaFold model) |
>4UEG_1 GLYCOGENIN-2 (chains A, B) MTDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSDLLRRILSKVFDEVIE VNLIDSADYIHLAFLKRPELGLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEF SAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIH KHLPFIYNLSSNTMYTYSPAFKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSVSSS QHQAAFLHLWWTVYQNNVLPLYKSVQAENLYFQSHHHHHHDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
Crystal Structure of Human Glycogenin-2 Catalytic Domain. Fairhead, M., Strain-Damerell, C., Krojer, T. et al. To be published.
Other PDB entries of the same protein (UniProt O15488 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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