Research workbench
Oxy hemoglobin (93% relative humidity)
Analyse Oxy hemoglobin (93% relative humidity) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LFQ
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin alpha chain; Hemoglobin beta chain
- UniProt
- P69905, P68871
- Ligands
- HEM
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin alpha chain | protein | 141 | 76% helix, 0% strand | P69905 |
| B | Hemoglobin beta chain | protein | 146 | 75% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.75 | 0.88 | 26 | HEM |
| 2 | 187 | 0.67 | 0.85 | 24 | HEM |
| 3 | 258 | 0.55 | 0.77 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 884 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1LFQ · Oxy hemoglobin (93% relative humidity) · 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 P69905
- Every structure of UniProt P68871
- Elsewhere: RCSB PDB 1LFQ · PDBe 1LFQ · UniProt P69905 · UniProt P68871
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