Research workbench
Rmlc from salmonella typhimurium
Analyse Rmlc from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DZR
- Type
- protein
- Length
- 366 residues
- Chains
- 2
- 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
- P26394
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dtdp-4-dehydrorhamnose 3\,5-epimerase (EC 5.1.3.13) | protein | 183 | 10% helix, 44% strand | P26394 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.75 | 0.98 | 22 | empty |
| 2 | 329 | 0.65 | 0.80 | 48 | GOL, SO4 |
| 3 | 275 | 0.64 | 0.81 | 47 | GOL, SO4 |
| 4 | 57 | 0.34 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1457 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
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 P26394
- Elsewhere: RCSB PDB 1DZR · PDBe 1DZR · UniProt P26394
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