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The high resolution structures of rmlc from streptococcus suis
Analyse The high resolution structures of rmlc from streptococcus suis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NXM
- Type
- protein
- Length
- 388 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dtdp-6-deoxy-D-xylo-4-hexulose 3,5-epimerase
- EC
- 5.1.3.13
- UniProt
- Q8GIQ0
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dtdp-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (EC 5.1.3.13) | protein | 194 | 12% helix, 40% strand | Q8GIQ0 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.54 | 0.77 | 35 | empty |
| 2 | 239 | 0.52 | 0.76 | 32 | empty |
| 3 | 65 | 0.50 | 0.85 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1427 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1NXM · The high resolution structures of RmlC from Streptococcus suis · 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 Q8GIQ0
- Elsewhere: RCSB PDB 1NXM · PDBe 1NXM · UniProt Q8GIQ0
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