Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP. Determined by X-ray diffraction at 2.26 Å resolution. Released 23 Mar 2011.
Explore 3QVB in 3D Show helices and sheets RCSB PDB PDBe
3QVB 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 | 45-51 | 7 | |
| β-strand | 57-60 | 4 | 1 |
| α-helix | 71-76 | 6 | |
| α-helix | 78-80 | 3 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-91 | 5 | |
| 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 | 199-204 | 6 | |
| α-helix | 205-207 | 3 | |
| β-strand | 210-212 | 3 | 2 |
| α-helix | 219-221 | 3 | |
| α-helix | 223 | 1 | |
| β-strand | 224-225 | 2 | 3 |
| β-strand | 230-231 | 2 | 3 |
| α-helix | 244-252 | 9 | |
| α-helix | 253-257 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogenin-1 | A | protein | 263 | Homo sapiens | P46976 (AlphaFold model) |
>3QVB_1 Glycogenin-1 (chains A) SMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVI MVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREE LSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDI RKHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPN MTHPEFLILWWNIFTTNVLPLLQ
Water and common crystallization additives (EDO) are not listed.
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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