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Crystal structure of human glycogenin-1 (GYG1) TYR195PIPHE mutant complexed with manganese and udp
Analyse Crystal structure of human glycogenin-1 (GYG1) TYR195PIPHE mutant complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EQL
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46976
- Ligands
- UDP, MN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 255 | — | P46976 |
| B | — | protein | 224 | — | P46976 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- 2PE · Nonaethylene glycol · additive · chains B
- EDO · 1,2-ethanediol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EQL · Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P46976 · AlphaFold monomer V2.0 prediction for glycogenin-1 (P46976) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P46976
- Elsewhere: RCSB PDB 6EQL · PDBe 6EQL · UniProt P46976
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