Research workbench
Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archeal and bacterial enzymes
Analyse Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XTZ
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribose-5-phosphate isomerase
- EC
- 5.3.1.6
- UniProt
- Q12189
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose-5-phosphate isomerase (EC 5.3.1.6) | protein | 246 | 29% helix, 29% strand | Q12189 |
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 | 85 | 0.40 | 0.79 | 24 | empty |
Compared structures
- 1XTZ · Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12189 · AlphaFold monomer V2.0 prediction for ribose-5-phosphate isomerase (Q12189) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q12189
- Elsewhere: RCSB PDB 1XTZ · PDBe 1XTZ · UniProt Q12189
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