Research workbench
Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin, hemoglobin exposed to no under aerobic conditions
Analyse Crystallographic analysis of the interaction of nitric oxide with quaternary-T… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RQ4
- Type
- protein
- Length
- 574 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin alpha chain; Hemoglobin beta chain
- UniProt
- P69905, P68871
- Ligands
- HEM, NO
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin alpha chain | protein | 141 | 73% helix, 0% strand | P69905 |
| B, D | Hemoglobin beta chain | protein | 146 | 77% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- NO · Nitric oxide · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 733 | 0.81 | 0.84 | 66 | empty |
| 2 | 256 | 0.74 | 0.87 | 30 | HEM, NO |
| 3 | 312 | 0.73 | 0.85 | 30 | HEM, NO |
| 4 | 257 | 0.73 | 0.86 | 29 | HEM, NO |
| 5 | 294 | 0.71 | 0.84 | 30 | HEM, NO |
Interfaces
5 interfaces between chains.
- A–B · 854 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 841 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 714 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 685 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 295 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
- 1RQ4 · Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human… · 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 1RQ4 · PDBe 1RQ4 · UniProt P69905 · UniProt P68871
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