Research workbench
Low resolution crystal structure of mouse rage
Analyse Low resolution crystal structure of mouse rage in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IM8
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Advanced glycation end-products receptor
- UniProt
- O35444
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Advanced glycation end-products receptor | protein | 198 | 2% helix, 45% strand | O35444 |
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 | 59 | 0.40 | 0.81 | 17 | empty |
| 2 | 57 | 0.27 | 0.73 | 14 | empty |
| 3 | 52 | 0.26 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4IM8 · low resolution crystal structure of mouse RAGE · 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 O35444
- Elsewhere: RCSB PDB 4IM8 · PDBe 4IM8 · UniProt O35444
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