Research workbench
Dini-sulerythrin treated by hydrogen perxoide
Analyse Dini-sulerythrin treated by hydrogen perxoide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O9C
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulerythrin
- UniProt
- F9VPE5
- Ligands
- NI, CL
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulerythrin | protein | 142 | 82% helix, 0% strand | F9VPE5 |
| B | Sulerythrin | protein | 145 | 81% helix, 0% strand | F9VPE5 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 5 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
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 | 91 | 0.43 | 0.79 | 19 | empty |
| 2 | 82 | 0.41 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3529 Ų buried · 54 hydrogen bonds · protein-protein
Compared structures
- 7O9C · diNi-sulerythrin treated by hydrogen perxoide · 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 F9VPE5
- Elsewhere: RCSB PDB 7O9C · PDBe 7O9C · UniProt F9VPE5
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