PDB ID
1HHO
Protein Name
Hemoglobin
Resolution
2.10 Å
Size (kDa)
64.5
3D Structure Visualization
Hemoglobin (α and β chains)
Source: RCSB PDB (1HHO)
Secondary Structure
Alpha Helix
72%
Beta Sheet
18%
Coil
10%
Physicochemical Properties
Molecular Weight
64.5 kDa
Theoretical pI
6.9
Instability Index
24.3 (stable)
Amino Acid Composition
>sp|P69905|HBA_HUMAN Hemoglobin subunit alpha OS=Homo sapiens OX=9606 GN=HBA1 PE=1 SV=2
MVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHG
KKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTP
AVHASLDKFLASVSTVLTSKYR
Sequence Features
Length
142 aa
Helices
7
Strands
0
Turns
12
Globin
7-138
PF00042
Heme binding
58-87
PS01033
Oxygen binding
92-99
PS01034
Protein-Protein Interactions
HBB_HUMAN
Hemoglobin subunit beta
Heme
Prosthetic group
Binding Sites
Heme binding site
His87
Oxygen binding site
His58
Protein Comparison
| Property | Hemoglobin (1HHO) | Myoglobin (1MBN) | Insulin (1TRZ) |
|---|---|---|---|
| Molecular Weight | 64.5 kDa | 17.2 kDa | 5.8 kDa |
| Resolution | 2.10 Å | 1.80 Å | 1.50 Å |
| Alpha Helix % | 72% | 75% | 60% |
| Beta Sheet % | 18% | 0% | 30% |
| Oligomer State | Tetramer | Monomer | Dimer |
References & Data Sources
- Berman, H.M., et al. (2000) The Protein Data Bank. Nucleic Acids Research, 28: 235-242.
- UniProt Consortium (2021) UniProt: the universal protein knowledgebase in 2021. Nucleic Acids Research, 49: D480-D489.
- Ferreira, A.M., et al. (2015) Hemoglobin stability and structure. Protein Science, 24: 1234-1246.
