Research workbench
The structure of human carbonmonoxyhemoglobin complex to ihp at 2.0 angstrons resolution.
Analyse The structure of human carbonmonoxyhemoglobin complex to ihp at 2.0 angstrons… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HXN
- Type
- protein
- Length
- 574 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, IHP, CMO
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hemoglobin subunit alpha | protein | 141 | 75% helix, 0% strand | P69905 |
| B, D | Hemoglobin subunit beta | protein | 146 | 75% helix, 0% strand | P68871 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- IHP · Inositol hexakisphosphate · ligand · chains B, D
- CMO · Carbon monoxide · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 895 | 0.82 | 0.84 | 85 | empty |
| 2 | 238 | 0.72 | 0.86 | 28 | HEM, CMO |
| 3 | 218 | 0.72 | 0.87 | 25 | HEM, CMO |
| 4 | 268 | 0.71 | 0.85 | 32 | HEM, CMO |
| 5 | 204 | 0.70 | 0.87 | 29 | HEM, CMO |
Interfaces
6 interfaces between chains.
- A–B · 861 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 853 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 708 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 697 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 282 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3HXN · The structure of human carbonmonoxyhemoglobin complex to IHP at 2.0 angstrons resolution. · 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 3HXN · PDBe 3HXN · UniProt P69905 · UniProt P68871
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