Research workbench
A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin
Analyse A cis-proline in alpha-hemoglobin stabilizing protein directs the structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IA3
- Type
- protein
- Length
- 450 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-hemoglobin-stabilizing protein; Hemoglobin subunit alpha
- UniProt
- Q9NZD4, P69905
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Alpha-hemoglobin-stabilizing protein | protein | 90 | 72% helix, 0% strand | Q9NZD4 |
| B, D | Hemoglobin subunit alpha | protein | 135 | 68% helix, 0% strand | P69905 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1160 | 0.88 | 0.88 | 140 | HEM |
| 2 | 50 | 0.31 | 0.77 | 20 | empty |
Interfaces
3 interfaces between chains.
- B–C · 958 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 942 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 750 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3IA3 · A cis-proline in alpha-hemoglobin stabilizing Protein directs the structural… · 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 0.95
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 3IA3 · PDBe 3IA3 · UniProt Q9NZD4 · UniProt P69905
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