Research workbench
Carbonmonoxy structure of the human fetal hemoglobin mutant hbf toms river ALPHAWTGAMMAV67M
Analyse Carbonmonoxy structure of the human fetal hemoglobin mutant hbf toms river… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MQK
- Type
- protein
- Length
- 1,140 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit gamma-2
- UniProt
- P69905, P69892
- Ligands
- HEM, CMO
- Pockets
- 16 · best druggability 0.89
Structure
x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin subunit alpha | protein | 141 | 77% helix, 0% strand | P69905 |
| B, D, F, H | Hemoglobin subunit gamma-2 | protein | 145 | 81% helix, 0% strand | P69892 |
| E | Hemoglobin subunit alpha | protein | 138 | 79% helix, 0% strand | P69905 |
| G | Hemoglobin subunit alpha | protein | 140 | 77% helix, 0% strand | P69905 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 8 copies · chains A, B, D, C, E, F, G, H
- CMO · Carbon monoxide · ion · 6 copies · chains A, B, C, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 940 | 0.89 | 0.90 | 95 | empty |
| 2 | 950 | 0.89 | 0.90 | 99 | empty |
| 3 | 1036 | 0.80 | 0.81 | 95 | HEM, CMO |
| 4 | 256 | 0.76 | 0.88 | 31 | HEM, CMO |
| 5 | 250 | 0.74 | 0.88 | 29 | HEM |
Interfaces
13 interfaces between chains.
- C–D · 868 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 866 Ų buried · 9 hydrogen bonds · protein-protein
- G–H · 854 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 854 Ų buried · 9 hydrogen bonds · protein-protein
- A–F · 530 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4MQK · Carbonmonoxy Structure of the Human Fetal Hemoglobin Mutant HbF Toms River… · the same entry in another collection · chain H against H, TM-score 1.00
- P69892 · AlphaFold monomer V2.0 prediction for hemoglobin subunit gamma-2 (P69892) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P69892
- Elsewhere: RCSB PDB 4MQK · PDBe 4MQK · UniProt P69905 · UniProt P69892
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