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Crystal structure of murine neuroglobin bound to CO at 40 K.
Analyse Crystal structure of murine neuroglobin bound to CO at 40 K. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I3T
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Mus musculus
- Molecule
- Neuroglobin
- UniProt
- Q9ER97
- Ligands
- HEM, CMO
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuroglobin | protein | 148 | 78% helix, 0% strand | Q9ER97 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CMO · Carbon monoxide · ion · chains A
- ACT · Acetate ion · additive · 4 copies · chains A
- FMT · Formic acid · additive · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
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 | 356 | 0.76 | 0.86 | 35 | HEM, CMO, FMT |
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 Q9ER97
- Elsewhere: RCSB PDB 6I3T · PDBe 6I3T · UniProt Q9ER97
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