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Crystal structure of the full-length human rage extracellular domain (VC1C2 fragment)
Analyse Crystal structure of the full-length human rage extracellular domain (VC1C2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LP5
- Type
- protein
- Length
- 513 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
- 4 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Advanced glycosylation end product-specific receptor | protein | 211 | 0% helix, 45% strand | Q15109 |
| A | Advanced glycosylation end product-specific receptor | protein | 302 | 2% helix, 48% strand | Q15109 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.49 | 0.79 | 20 | empty |
| 2 | 83 | 0.39 | 0.77 | 18 | empty |
| 3 | 86 | 0.33 | 0.74 | 22 | empty |
| 4 | 64 | 0.28 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- B–A · 683 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 4LP5 · Crystal structure of the full-length human RAGE extracellular domain (VC1C2 fragment) · the same entry in another collection · chain B against B, TM-score 1.00
- Q15109 · AlphaFold monomer V2.0 prediction for advanced glycosylation end product-specific… · a predicted model of the same protein · chain B 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 Q15109
- Elsewhere: RCSB PDB 4LP5 · PDBe 4LP5 · UniProt Q15109
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