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Structures and oxygen affinities of crystalline human hemoglobin C (BETA6 lys) in the R quaternary structures
Analyse Structures and oxygen affinities of crystalline human hemoglobin C (BETA6 lys)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S66
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta
- UniProt
- P69905, P68871
- Ligands
- HEM, CMO
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin subunit alpha | protein | 139 | 75% helix, 0% strand | P69905 |
| B | Hemoglobin subunit beta | protein | 146 | 78% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CMO · Carbon monoxide · 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 | 227 | 0.73 | 0.87 | 27 | HEM, CMO |
| 2 | 206 | 0.71 | 0.86 | 24 | HEM, CMO |
| 3 | 113 | 0.54 | 0.83 | 22 | empty |
| 4 | 78 | 0.37 | 0.77 | 21 | empty |
| 5 | 76 | 0.32 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 941 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3S66 · Structures and oxygen affinities of crystalline human hemoglobin C (beta6 Lys) in the R… · 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 3S66 · PDBe 3S66 · UniProt P69905 · UniProt P68871
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