Research workbench
Domain of unknown function 1792 (DUF1792) with manganese
Analyse Domain of unknown function 1792 (DUF1792) with manganese in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PHR
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative glycosyltransferase (GALT1)
- UniProt
- I1ZPA1
- Ligands
- UDP, MN
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative glycosyltransferase (GALT1) | protein | 277 | 42% helix, 16% strand | I1ZPA1 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.79 | 0.88 | 53 | UDP, MN, ACT |
| 2 | 59 | 0.30 | 0.75 | 17 | empty |
Compared structures
- 4PHR · Domain of unknown function 1792 (DUF1792) with manganese · the same entry in another collection · chain A against A, 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 I1ZPA1
- Elsewhere: RCSB PDB 4PHR · PDBe 4PHR · UniProt I1ZPA1
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