Research workbench
Substrate and inhibitor complexes of ribose 5-phosphate isomerase from vibrio vulnificus YJ016
Analyse Substrate and inhibitor complexes of ribose 5-phosphate isomerase from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ENW
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribose-5-phosphate isomerase a
- EC
- 5.3.1.6
- UniProt
- Q7MHL9
- Ligands
- 5RP
- Pockets
- 6 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribose-5-phosphate isomerase a (EC 5.3.1.6) | protein | 217 | 34% helix, 28% strand | Q7MHL9 |
Ligands and binding sites
- 5RP · Ribulose-5-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.44 | 0.80 | 24 | empty |
| 2 | 90 | 0.41 | 0.78 | 20 | empty |
| 3 | 78 | 0.41 | 0.79 | 19 | 5RP |
| 4 | 82 | 0.39 | 0.78 | 18 | empty |
| 5 | 65 | 0.37 | 0.79 | 18 | 5RP |
Interfaces
1 interface between chains.
- A–B · 1195 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3ENW · Substrate and inhibitor complexes of ribose 5-phosphate isomerase from Vibrio vulnificus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q7MHL9 · AlphaFold monomer V2.0 prediction for ribose-5-phosphate isomerase a (Q7MHL9) · 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 Q7MHL9
- Elsewhere: RCSB PDB 3ENW · PDBe 3ENW · UniProt Q7MHL9
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