MolNFT v1 · #43268 · protein
Structure of cel-pep-rage V domain complex
2L7U · Advanced glycosylation end product-specific receptor: “Structure of cel-pep-rage V domain complex”. Solution nmr, 2 pockets (best druggability 0.40). MolNFT v1 #43268 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2L7U
- Type
- protein
- Length
- 112 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Advanced glycosylation end product-specific receptor; Serum albumin peptide
- UniProt
- Q15109, P02769
- Pockets
- 2 · best druggability 0.40
Structure
solution nmr · 2 distinct chains · 3% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Advanced glycosylation end product-specific receptor | protein | 105 | 3% helix, 41% strand | Q15109 |
| B | Serum albumin peptide | protein | 7 | 0% helix, 0% strand | P02769 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.40 | 0.81 | 16 | empty |
| 2 | 59 | 0.33 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 426 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 2L7U · Structure of CEL-PEP-RAGE V domain complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q15109 · AlphaFold monomer V2.0 prediction for advanced glycosylation end product-specific… · a predicted model of the same protein · chain A against A, TM-score 0.75
- P02769 · AlphaFold monomer V2.0 prediction for albumin (P02769) · a predicted model of the same protein · chain B against A, TM-score 0.42
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
- Every structure of UniProt P02769
- Elsewhere: RCSB PDB 2L7U · PDBe 2L7U · UniProt Q15109 · UniProt P02769
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