MolNFT v1 · #27949 · protein
Wild-type hemoglobin deoxy no-salt
1XZ2 · Hemoglobin alpha chain: “Wild-type hemoglobin deoxy no-salt”. X-ray diffraction, 1 ligand (HEM), 10 pockets (best druggability 0.79). MolNFT v1 #27949 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1XZ2
- 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
- 10 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin alpha chain | protein | 141 | 78% helix, 0% strand | P01922 |
| B, D | Hemoglobin beta chain | protein | 146 | 82% 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
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1113 | 0.79 | 0.81 | 87 | empty |
| 2 | 283 | 0.73 | 0.86 | 30 | HEM |
| 3 | 273 | 0.72 | 0.85 | 32 | HEM |
| 4 | 227 | 0.71 | 0.86 | 27 | HEM |
| 5 | 219 | 0.71 | 0.86 | 26 | HEM |
Interfaces
5 interfaces between chains.
- C–D · 842 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 834 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 718 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 718 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 307 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1XZ2 · wild-type hemoglobin deoxy no-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 1XZ2 · PDBe 1XZ2 · UniProt P01922 · UniProt P68871
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