Research workbench
Human udp-glucose dehydrogenase A225L substitutuion with udp-xylose bound
Analyse Human udp-glucose dehydrogenase A225L substitutuion with udp-xylose bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C58
- Type
- protein
- Length
- 2,736 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60701
- Ligands
- UDX, CL
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 461 | — | O60701 |
| B, F | — | protein | 459 | — | O60701 |
| C | — | protein | 461 | — | O60701 |
| D | — | protein | 449 | — | O60701 |
| E | — | protein | 447 | — | O60701 |
Ligands and binding sites
- UDX · Uridine-5'-diphosphate-xylopyranose · ligand · 10 copies · chains A, B, C, D, E, F
- CL · Chloride ion · ion · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C58 · Human UDP-Glucose Dehydrogenase A225L substitutuion with UDP-xylose bound · the same entry in another collection · chain B against B, TM-score 1.00
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 6C58 · PDBe 6C58 · UniProt O60701
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