Research workbench
2.05 ångström resolution crystal structure of D-ribulose-phosphate 3- epimerase from francisella tularensis.
Analyse 2.05 ångström resolution crystal structure of D-ribulose-phosphate 3- epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3INP
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-ribulose-phosphate 3-epimerase
- EC
- 5.1.3.1
- UniProt
- Q5NGP6
- Ligands
- CL, SO4
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-ribulose-phosphate 3-epimerase (EC 5.1.3.1) | protein | 218 | 42% helix, 20% strand | Q5NGP6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.51 | 0.79 | 26 | SO4 |
Compared structures
- 3INP · 2.05 Angstrom Resolution Crystal Structure of D-ribulose-phosphate 3-epimerase from… · 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 Q5NGP6
- Elsewhere: RCSB PDB 3INP · PDBe 3INP · UniProt Q5NGP6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.