MolNFT v1 · #19278 · protein
Histamine binding protein from female brown ear rhipicephalus appendiculatus
1QFT · Protein (female-specific histamine binding protein 2): “Histamine binding protein from female brown ear rhipicephalus appendiculatus”. X-ray diffraction, 1 ligand (HSM), 1 pocket (best druggability 0.43). MolNFT v1 #19278 on…
- PDB
- 1QFT
- Type
- protein
- Length
- 344 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (female-specific histamine binding protein 2)
- UniProt
- O77421
- Ligands
- HSM
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (female-specific histamine binding protein 2) | protein | 175 | 17% helix, 44% strand | O77421 |
| B | Protein (female-specific histamine binding protein 2) | protein | 169 | 14% helix, 41% strand | O77421 |
Ligands and binding sites
- HSM · Histamine · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.43 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 369 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1QFT · Histamine binding protein from female brown ear rhipicephalus appendiculatus · the same entry in another collection · chain A against A, TM-score 1.00
- O77421 · AlphaFold monomer V2.0 prediction for female-specific histamine- binding protein 2… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O77421
- Elsewhere: RCSB PDB 1QFT · PDBe 1QFT · UniProt O77421
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