MolNFT v1 · #172689 · protein
Structure of human PERP1
7AAH · Marginal zone B- and B1-cell-specific protein: “Structure of human PERP1”. X-ray diffraction, 4 pockets (best druggability 0.63). MolNFT v1 #172689 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AAH
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Marginal zone B- and B1-cell-specific protein
- UniProt
- Q8WU39
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Marginal zone B- and B1-cell-specific protein | protein | 147 | 48% helix, 14% strand | Q8WU39 |
| B | Marginal zone B- and B1-cell-specific protein | protein | 139 | 53% helix, 12% strand | Q8WU39 |
Ligands and binding sites
- CIT · Citric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 450 | 0.63 | 0.77 | 61 | empty |
| 2 | 140 | 0.38 | 0.73 | 29 | empty |
| 3 | 78 | 0.33 | 0.75 | 16 | empty |
| 4 | 59 | 0.30 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1028 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
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 Q8WU39
- Elsewhere: RCSB PDB 7AAH · PDBe 7AAH · UniProt Q8WU39
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.