Research workbench
Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore beroe abyssicola in the CA2+-loaded apoprotein conformation state
Analyse Spatial structure of the novel light-sensitive photoprotein berovin from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MN0
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Berovin
- UniProt
- H8ZZK1
- Ligands
- CA, MG
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Berovin | protein | 182 | 61% helix, 4% strand | H8ZZK1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.64 | 0.82 | 26 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4MN0 · Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore… · 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 H8ZZK1
- Elsewhere: RCSB PDB 4MN0 · PDBe 4MN0 · UniProt H8ZZK1
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