Research workbench
Crystal structure of human udp-glucose dehydrogenase GLU161GLN, in complex with thiohemiacetal intermediate
Analyse Crystal structure of human udp-glucose dehydrogenase GLU161GLN, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KHU
- Type
- protein
- Length
- 2,789 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60701
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 463 | — | O60701 |
| B, C | — | protein | 467 | — | O60701 |
| D | — | protein | 464 | — | O60701 |
| E | — | protein | 466 | — | O60701 |
| F | — | protein | 462 | — | O60701 |
Compared structures
- 3KHU · Crystal structure of human UDP-glucose dehydrogenase Glu161Gln, in complex with… · the same entry in another collection · chain F against F, TM-score 1.00
- O60701 · AlphaFold monomer V2.0 prediction for udp-glucose 6-dehydrogenase (O60701) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O60701
- Elsewhere: RCSB PDB 3KHU · PDBe 3KHU · UniProt O60701
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