MolNFT v1 · #114017 · protein
Crystal structure of lgg-2 fused with an eeeweel peptide
5AZH · Eeeweel PEPTIDE,PROTEIN lgg-2: “Crystal structure of lgg-2 fused with an eeeweel peptide”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.41). MolNFT v1 #114017 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5AZH
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eeeweel PEPTIDE,PROTEIN lgg-2
- UniProt
- Q23536
- Ligands
- MG
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eeeweel PEPTIDE,PROTEIN lgg-2 | protein | 127 | 30% helix, 21% strand | Q23536 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.41 | 0.74 | 31 | empty |
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 Q23536
- Elsewhere: RCSB PDB 5AZH · PDBe 5AZH · UniProt Q23536
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