Research workbench
Structure of myohemerythrin in the azidomet state at 1.7(SLASH)1.3 ångströms resolution
Analyse Structure of myohemerythrin in the azidomet state at 1.7(SLASH)1.3 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MHR
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.3
- Source
- Themiste zostericola
- Molecule
- Myohemerythrin
- UniProt
- P02247
- Ligands
- FEO, SO4, AZI
Structure
x-ray diffraction · resolution 1.3 · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myohemerythrin | protein | 118 | 70% helix, 0% strand | P02247 |
Ligands and binding sites
- FEO · Mu-oxo-diiron · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- AZI · Azide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2MHR · Structure of myohemerythrin in the azidomet state at 1.7(SLASH)1.3 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P02247 · AlphaFold monomer V2.0 prediction for myohemerythrin (P02247) · a predicted model of the same protein · 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 P02247
- Elsewhere: RCSB PDB 2MHR · PDBe 2MHR · UniProt P02247
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