MolNFT v1 · #98958 · protein
Crystal structure of the full-length human rage extracellular domain (VC1C2 fragment)
4LP5: “Crystal structure of the full-length human rage extracellular domain (VC1C2 fragment)”. X-ray diffraction. MolNFT v1 #98958 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4LP5
- Type
- protein
- Length
- 513 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15109
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 211 | — | Q15109 |
| A | — | protein | 302 | — | Q15109 |
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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