Research workbench
Structure of the T. brucei haptoglobin-haemoglobin receptor bound to human haptolgobin-haemoglobin
Analyse Structure of the T. brucei haptoglobin-haemoglobin receptor bound to human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HU6
- Type
- protein
- Length
- 784 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta; Haptoglobin; Haptoglobin-hemoglobin…
- UniProt
- P69905, P68871, P00738, I7B1A7
- Ligands
- HEM, NAG, OXY
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin subunit alpha | protein | 141 | 78% helix, 0% strand | P69905 |
| B | Hemoglobin subunit beta | protein | 141 | 77% helix, 0% strand | P68871 |
| C | Haptoglobin | protein | 242 | 15% helix, 31% strand | P00738 |
| D | Haptoglobin-hemoglobin receptor | protein | 260 | 87% helix, 0% strand | I7B1A7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains C
- OXY · Oxygen molecule · ion · 2 copies · chains A, B
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 | 1089 | 0.81 | 0.82 | 113 | empty |
| 2 | 412 | 0.79 | 0.87 | 40 | HEM, OXY |
| 3 | 228 | 0.73 | 0.87 | 25 | HEM, OXY |
| 4 | 379 | 0.66 | 0.80 | 45 | empty |
| 5 | 221 | 0.63 | 0.82 | 33 | empty |
Interfaces
5 interfaces between chains.
- A–B · 868 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 856 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 673 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 584 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 526 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
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
- Every structure of UniProt P00738
- Every structure of UniProt I7B1A7
- Elsewhere: RCSB PDB 5HU6 · PDBe 5HU6 · UniProt P69905 · UniProt P68871 · UniProt P00738 · UniProt I7B1A7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.