MolNFT v1 · #189177 · protein
Structure of adav
7V52: “Structure of adav”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.48). MolNFT v1 #189177 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7V52
- Type
- protein
- Length
- 267 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adav
- UniProt
- A0A1U8X168
- Ligands
- FE
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adav | protein | 267 | 35% helix, 26% strand | A0A1U8X168 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 125 | 0.48 | 0.79 | 21 | FE |
| 2 | 86 | 0.43 | 0.79 | 25 | empty |
Compared structures
- 7V52 · Structure of AdaV · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A1U8X168
- Elsewhere: RCSB PDB 7V52 · PDBe 7V52 · UniProt A0A1U8X168
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