Research workbench
High resolution crystal structure of hemoglobin M boston.
Analyse High resolution crystal structure of hemoglobin M boston. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DY4
- Type
- protein
- Length
- 1,148 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta
- UniProt
- P69905, P68871
- Ligands
- HEM
- Pockets
- 18 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Hemoglobin subunit alpha | protein | 141 | 79% helix, 0% strand | P69905 |
| B, D, F, H | Hemoglobin subunit beta | protein | 146 | 78% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1080 | 0.81 | 0.82 | 86 | empty |
| 2 | 1199 | 0.81 | 0.82 | 88 | empty |
| 3 | 1034 | 0.74 | 0.77 | 108 | empty |
| 4 | 227 | 0.74 | 0.88 | 28 | HEM |
| 5 | 217 | 0.72 | 0.87 | 25 | HEM |
Interfaces
13 interfaces between chains.
- E–F · 862 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 849 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 847 Ų buried · 9 hydrogen bonds · protein-protein
- G–H · 840 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 710 Ų buried · 8 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 P69905
- Every structure of UniProt P68871
- Elsewhere: RCSB PDB 7DY4 · PDBe 7DY4 · UniProt P69905 · UniProt P68871
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