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Crystal structure of deoxygenated hemoglobin in complex with an allosteric effector and nitric oxide
Analyse Crystal structure of deoxygenated hemoglobin in complex with an allosteric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E29
- Type
- protein
- Length
- 572 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta
- UniProt
- P69905, P68871
- Ligands
- HEM, RQ3, 5JN, NO, NO3
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin subunit alpha | protein | 141 | 78% helix, 0% strand | P69905 |
| B, D | Hemoglobin subunit beta | protein | 145 | 79% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- RQ3 · 2-{4-[(3,5-dimethylanilino)-carbonyl-methyl]-phenoxy}-2-methylpropionic acid · ligand · 2 copies · chains A, C, D, B
- 5JN · 2-(nitrooxy)ethyl 2-(4-{2-[(3,5-dimethylphenyl)amino]-2-oxoethyl}phenoxy)-2-methylpropanoate · ligand · chains A, B, C
- NO · Nitric oxide · ion · 2 copies · chains A, C
- NO3 · Nitrate ion · ion · 2 copies · chains B, C, D
- CAC · Cacodylate ion · additive · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1067 | 0.80 | 0.81 | 78 | 5JN, RQ3 |
| 2 | 225 | 0.73 | 0.88 | 31 | HEM |
| 3 | 226 | 0.73 | 0.87 | 31 | HEM |
| 4 | 259 | 0.71 | 0.85 | 29 | NO, HEM |
| 5 | 263 | 0.70 | 0.84 | 33 | NO, HEM |
Interfaces
5 interfaces between chains.
- A–B · 844 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 840 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 711 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 698 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 294 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5E29 · Crystal Structure of Deoxygenated Hemoglobin in Complex with an Allosteric Effector and… · 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 5E29 · PDBe 5E29 · UniProt P69905 · UniProt P68871
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