Research workbench
Crystal Structure of Horse heart ferric myoglobin; K45E/K63E/K96E mutant
Analyse Crystal Structure of Horse heart ferric myoglobin; K45E/K63E/K96E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RJ6
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.23
- Source
- Equus caballus
- Molecule
- Myoglobin
- UniProt
- P68082
- Ligands
- HEM, SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · resolution 1.23 · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Myoglobin | protein | 153 | 75% helix, 0% strand | P68082 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.72 | 0.87 | 27 | HEM |
| 2 | 217 | 0.72 | 0.87 | 28 | HEM |
| 3 | 56 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 519 Ų buried · 8 hydrogen bonds · protein-protein
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 P68082
- Elsewhere: RCSB PDB 3RJ6 · PDBe 3RJ6 · UniProt P68082
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