MolNFT v1 · #19350 · protein
Mammalian blood serum haemopexin deglycosylated and in complex with its ligand haem
1QHU · Protein (hemopexin): “Mammalian blood serum haemopexin deglycosylated and in complex with its ligand haem”. X-ray diffraction, 4 ligands (HEM, NA, CL), 4 pockets (best druggability 0.59). MolNFT v1 #19350 on GenesisL1: 3D structure…
- PDB
- 1QHU
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (hemopexin)
- UniProt
- P20058
- Ligands
- HEM, NA, CL, PO4
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (hemopexin) | protein | 398 | 11% helix, 38% strand | P20058 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NA · Sodium ion · metal · 4 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.59 | 0.80 | 43 | empty |
| 2 | 296 | 0.53 | 0.74 | 33 | HEM |
| 3 | 75 | 0.37 | 0.77 | 17 | empty |
| 4 | 65 | 0.34 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1QHU · Mammalian blood serum haemopexin deglycosylated and in complex with its ligand haem · the same entry in another collection · chain A against A, TM-score 1.00
- P20058 · AlphaFold monomer V2.0 prediction for hemopexin (P20058) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P20058
- Elsewhere: RCSB PDB 1QHU · PDBe 1QHU · UniProt P20058
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