Research workbench
The structure of ascaris hemoglobin domain I at 2.2 ångströms resolution: molecular features of oxygen avidity
Analyse The structure of ascaris hemoglobin domain I at 2.2 ångströms resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ASH
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin (oxy)
- UniProt
- P28316
- Ligands
- HEM, OXY
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin (oxy) | protein | 147 | 78% helix, 0% strand | P28316 |
Ligands and binding sites
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 | 302 | 0.73 | 0.85 | 31 | HEM, OXY |
Compared structures
- 1ASH · The structure of ascaris hemoglobin domain I at 2.2 ångströms resolution: molecular… · the same entry in another collection · chain A against A, TM-score 1.00
- P28316 · AlphaFold monomer V2.0 prediction for extracellular globin (P28316) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P28316
- Elsewhere: RCSB PDB 1ASH · PDBe 1ASH · UniProt P28316
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