Research workbench
Isolated globin domain of the bordetella pertussis globin-coupled sensor
Analyse Isolated globin domain of the bordetella pertussis globin-coupled sensor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I2Z
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q7VTL8
- Ligands
- HEM
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 155 | 77% helix, 0% strand | Q7VTL8 |
| B | Uncharacterized protein | protein | 151 | 83% helix, 0% strand | Q7VTL8 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.75 | 0.86 | 31 | HEM |
| 2 | 353 | 0.73 | 0.84 | 41 | HEM |
| 3 | 165 | 0.65 | 0.86 | 39 | empty |
| 4 | 74 | 0.30 | 0.73 | 13 | empty |
| 5 | 54 | 0.26 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1137 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6I2Z · Isolated globin domain of the Bordetella pertussis globin-coupled sensor · 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 Q7VTL8
- Elsewhere: RCSB PDB 6I2Z · PDBe 6I2Z · UniProt Q7VTL8
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