Research workbench
High resolutionstructure of apo dtdp-4-dehydrorhamnose 3,5-epimerase
Analyse High resolutionstructure of apo dtdp-4-dehydrorhamnose 3,5-epimerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DIN
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dtdp-4-dehydrorhamnose 3,5-epimerase
- EC
- 5.1.3.13
- UniProt
- A0A0D6IV69
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) | protein | 184 | 10% helix, 44% strand | A0A0D6IV69 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.47 | 0.79 | 23 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 6DIN · High resolutionstructure of apo dTDP-4-dehydrorhamnose 3,5-epimerase · 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 A0A0D6IV69
- Elsewhere: RCSB PDB 6DIN · PDBe 6DIN · UniProt A0A0D6IV69
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