Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant complexed with manganese and UDP. Determined by X-ray diffraction at 1.82 Å resolution. Released 18 May 2011.
Explore 3RMV in 3D Show helices and sheets RCSB PDB PDBe
3RMV 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 | 45-54 | 10 | |
| β-strand | 57-60 | 4 | 1 |
| α-helix | 71-76 | 6 | |
| 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 | 164-170 | 7 | |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 1 |
| α-helix | 185-187 | 3 | |
| β-strand | 189 | 1 | 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 | |
| α-helix | 258-261 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogenin-1 | A | protein | 263 | Homo sapiens | P46976 (AlphaFold model) |
>3RMV_1 Glycogenin-1 (chains A) SMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVI MVDVLDSGDSAHLTLMKRPELGVMLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREE LSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDI RKHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPN MTHPEFLILWWNIFTTNVLPLLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| UDP | Uridine-5'-diphosphate | C9 H14 N2 O12 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| MN | Manganese (II) ion | Mn | 1 |
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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