Research workbench
D-ribose-binding protein from escherichia COLI
Analyse D-ribose-binding protein from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1URP
- Type
- protein
- Length
- 1,084 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-ribose-binding protein
- UniProt
- P02925
- Pockets
- 11 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | D-ribose-binding protein | protein | 271 | 46% helix, 20% strand | P02925 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 663 | 0.68 | 0.77 | 69 | empty |
| 2 | 233 | 0.68 | 0.85 | 34 | empty |
| 3 | 187 | 0.54 | 0.79 | 30 | empty |
| 4 | 260 | 0.54 | 0.76 | 33 | empty |
| 5 | 255 | 0.53 | 0.76 | 36 | empty |
Interfaces
4 interfaces between chains.
- B–D · 808 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 174 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 169 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 55 Ų buried · 0 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 P02925
- Elsewhere: RCSB PDB 1URP · PDBe 1URP · UniProt P02925
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