MolNFT v1 · #27926 · protein
T-to-thigh transitions in human hemoglobin: alpha Y42A deoxy low salt
1XYE · Hemoglobin alpha chain: “T-to-thigh transitions in human hemoglobin: alpha Y42A deoxy low salt”. X-ray diffraction, 1 ligand (HEM), 9 pockets (best druggability 0.80). MolNFT v1 #27926 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1XYE
- Type
- protein
- Length
- 574 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin alpha chain; Hemoglobin beta chain
- UniProt
- P01922, P68871
- Ligands
- HEM
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin alpha chain | protein | 141 | 74% helix, 0% strand | P01922 |
| B, D | Hemoglobin beta chain | protein | 146 | 77% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.80 | 0.81 | 91 | empty |
| 2 | 272 | 0.74 | 0.87 | 32 | HEM |
| 3 | 252 | 0.72 | 0.86 | 29 | HEM |
| 4 | 242 | 0.71 | 0.85 | 29 | HEM |
| 5 | 279 | 0.71 | 0.84 | 34 | HEM |
Interfaces
5 interfaces between chains.
- C–D · 847 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 845 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 698 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 685 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 287 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1XYE · T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt · the same entry in another collection · 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 P01922
- Every structure of UniProt P68871
- Elsewhere: RCSB PDB 1XYE · PDBe 1XYE · UniProt P01922 · UniProt P68871
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