Research workbench
Crystal structure of the insect immune protein hemolin: a new domain arrangement with implications for homophilic adhesion
Analyse Crystal structure of the insect immune protein hemolin: a new domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BIH
- Type
- protein
- Length
- 782 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolin
- UniProt
- P25033
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hemolin | protein | 391 | 3% helix, 50% strand | P25033 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.66 | 0.78 | 51 | empty |
| 2 | 284 | 0.65 | 0.81 | 48 | empty |
| 3 | 75 | 0.50 | 0.84 | 20 | empty |
| 4 | 187 | 0.43 | 0.73 | 29 | empty |
| 5 | 72 | 0.38 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1476 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1BIH · Crystal structure of the insect immune protein hemolin: a new domain arrangement with… · the same entry in another collection · chain A against A, TM-score 1.00
- P25033 · AlphaFold monomer V2.0 prediction for hemolin (P25033) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P25033
- Elsewhere: RCSB PDB 1BIH · PDBe 1BIH · UniProt P25033
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