Research workbench
Human azido-met hemoglobin BART'S (GAMMA4)
Analyse Human azido-met hemoglobin BART'S (GAMMA4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I3E
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin gamma chains
- UniProt
- P69891
- Ligands
- HEM, AZI
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hemoglobin gamma chains | protein | 146 | 84% helix, 0% strand | P69891 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- AZI · Azide ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.75 | 0.88 | 29 | AZI, HEM |
| 2 | 214 | 0.72 | 0.87 | 29 | AZI, HEM |
| 3 | 157 | 0.51 | 0.79 | 41 | empty |
| 4 | 70 | 0.35 | 0.76 | 21 | empty |
| 5 | 55 | 0.26 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 866 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 P69891
- Elsewhere: RCSB PDB 1I3E · PDBe 1I3E · UniProt P69891
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