Research workbench
Structure of the haptoglobin-haemoglobin complex
Analyse Structure of the haptoglobin-haemoglobin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F4O
- Type
- protein
- Length
- 2,384 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin subunit alpha; Hemoglobin subunit beta; Haptoglobin
- UniProt
- P01965, P02067, Q8SPS7
- Ligands
- HEM, NAG, FUC, OXY
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Hemoglobin subunit alpha | protein | 141 | 76% helix, 0% strand | P01965 |
| B, E, H, K | Hemoglobin subunit beta | protein | 146 | 77% helix, 0% strand | P02067 |
| C, F, I, L | Haptoglobin | protein | 309 | 11% helix, 33% strand | Q8SPS7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 8 copies · chains A, B, D, E, G, H, J, K
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains C, A, B, F, E, I, H, K, L
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains C, F, I, L
- OXY · Oxygen molecule · ion · 8 copies · chains A, B, D, E, G, H, J, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.75 | 0.88 | 28 | HEM, OXY |
| 2 | 207 | 0.73 | 0.88 | 28 | HEM, OXY |
| 3 | 234 | 0.72 | 0.87 | 27 | HEM, OXY |
| 4 | 206 | 0.72 | 0.88 | 26 | HEM, OXY |
| 5 | 229 | 0.72 | 0.87 | 27 | HEM, OXY |
Interfaces
15 interfaces between chains.
- I–L · 1562 Ų buried · 23 hydrogen bonds · protein-protein
- C–F · 1528 Ų buried · 22 hydrogen bonds · protein-protein
- J–K · 914 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 901 Ų buried · 9 hydrogen bonds · protein-protein
- G–H · 900 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 15 glycan (disulfide, N-glycosylation).
Compared structures
- 4F4O · Structure of the Haptoglobin-Haemoglobin Complex · the same entry in another collection · chain L against L, 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 P01965
- Every structure of UniProt P02067
- Every structure of UniProt Q8SPS7
- Elsewhere: RCSB PDB 4F4O · PDBe 4F4O · UniProt P01965 · UniProt P02067 · UniProt Q8SPS7
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