Research workbench
Refinement of rage-DNA complex in 3S58 without DNA
Analyse Refinement of rage-DNA complex in 3S58 without DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OFV
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Advanced glycosylation end product-specific receptor
- UniProt
- Q15109
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Advanced glycosylation end product-specific receptor | protein | 211 | 1% helix, 49% strand | Q15109 |
| B | Advanced glycosylation end product-specific receptor | protein | 215 | 1% helix, 48% strand | Q15109 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.42 | 0.77 | 17 | empty |
| 2 | 81 | 0.40 | 0.78 | 22 | empty |
| 3 | 62 | 0.40 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 612 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q15109
- Elsewhere: RCSB PDB 4OFV · PDBe 4OFV · UniProt Q15109
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