Research workbench
Crystal structure of ahsp bound to FE(II) alpha-hemoglobin
Analyse Crystal structure of ahsp bound to FE(II) alpha-hemoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y01
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-hemoglobin stabilizing protein; Hemoglobin alpha chain
- UniProt
- Q9NZD4, P69905
- Ligands
- HEM, CHK, OXY
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-hemoglobin stabilizing protein | protein | 89 | 76% helix, 0% strand | Q9NZD4 |
| B | Hemoglobin alpha chain | protein | 126 | 72% helix, 0% strand | P69905 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains B
- CHK · 6-[(cyclohexylacetyl)(2-hydroxyethyl)amino]-6-deoxy-D-xylo-hexitol · ligand · chains B
- OXY · Oxygen molecule · ion · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 292 | 0.68 | 0.82 | 33 | HEM, OXY |
| 2 | 61 | 0.45 | 0.83 | 11 | empty |
| 3 | 64 | 0.35 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 882 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1Y01 · Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NZD4 · AlphaFold monomer V2.0 prediction for alpha-hemoglobin-stabilizing protein (Q9NZD4) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q9NZD4
- Every structure of UniProt P69905
- Elsewhere: RCSB PDB 1Y01 · PDBe 1Y01 · UniProt Q9NZD4 · UniProt P69905
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