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Crystal structure of human glycogenin-2 catalytic domain
Analyse Crystal structure of human glycogenin-2 catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UEG
- Type
- protein
- Length
- 491 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogenin-2
- EC
- 2.4.1.186
- UniProt
- O15488
- Ligands
- MG
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogenin-2 (EC 2.4.1.186) | protein | 242 | 45% helix, 17% strand | O15488 |
| B | Glycogenin-2 (EC 2.4.1.186) | protein | 249 | 45% helix, 17% strand | O15488 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.76 | 0.85 | 49 | MG |
| 2 | 272 | 0.64 | 0.81 | 35 | empty |
| 3 | 62 | 0.51 | 0.86 | 18 | empty |
| 4 | 196 | 0.49 | 0.76 | 22 | MG |
Interfaces
1 interface between chains.
- A–B · 1042 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O15488
- Elsewhere: RCSB PDB 4UEG · PDBe 4UEG · UniProt O15488
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