Crystal Structure of Human Glycogenin-1 (GYG1), apo form. Determined by X-ray diffraction at 1.98 Å resolution. Released 9 Feb 2011.
Explore 3Q4S in 3D Show helices and sheets RCSB PDB PDBe
3Q4S contains 18 α-helices and 12 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 |
|---|---|---|---|
| β-strand | 1-10 | 10 | 1 |
| α-helix | 13-28 | 16 | |
| β-strand | 33-39 | 7 | 1 |
| α-helix | 45-52 | 8 | |
| β-strand | 57-60 | 4 | 1 |
| α-helix | 71-76 | 6 | |
| α-helix | 78-80 | 3 | |
| α-helix | 81-87 | 7 | |
| α-helix | 88-91 | 4 | |
| β-strand | 97-101 | 5 | 1 |
| β-strand | 105-107 | 3 | 2 |
| α-helix | 112-116 | 5 | |
| β-strand | 121-124 | 4 | 1 |
| α-helix | 125 | 1 | |
| β-strand | 132-139 | 8 | 1 |
| α-helix | 143-156 | 14 | |
| α-helix | 163-170 | 8 | |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 1 |
| α-helix | 185-187 | 3 | |
| β-strand | 189-190 | 2 | 2 |
| α-helix | 198-204 | 7 | |
| α-helix | 205-207 | 3 | |
| β-strand | 210-212 | 3 | 2 |
| α-helix | 219-221 | 3 | |
| β-strand | 224-225 | 2 | 3 |
| β-strand | 230-231 | 2 | 3 |
| α-helix | 244-252 | 9 | |
| α-helix | 253-257 | 5 | |
| α-helix | 258-260 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogenin-1 | A | protein | 263 | Homo sapiens | P46976 (AlphaFold model) |
>3Q4S_1 Glycogenin-1 (chains A) SMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVI MVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREE LSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDI RKHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPN MTHPEFLILWWNIFTTNVLPLLQ
Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis. Chaikuad, A., Froese, D.S., Berridge, G. et al. Proc Natl Acad Sci U S A (2011) 108:21028-21033. DOI 10.1073/pnas.1113921108 · PubMed
Other PDB entries of the same protein (UniProt P46976 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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