Research workbench
EGF domains 1,2,5 of human EMR2, a 7-tm immune system molecule, in complex with calcium.
Analyse EGF domains 1,2,5 of human EMR2, a 7-tm immune system molecule, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BO2
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EGF-like module containing mucin-like hormone receptor-like 2 precursor
- UniProt
- Q9UHX3
- Ligands
- CA
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EGF-like module containing mucin-like hormone receptor-like 2 precursor | protein | 140 | 2% helix, 31% strand | Q9UHX3 |
| B | EGF-like module containing mucin-like hormone receptor-like 2 precursor | protein | 138 | 2% helix, 31% strand | Q9UHX3 |
Ligands and binding sites
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 | 76 | 0.43 | 0.81 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 500 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
- 2BO2 · EGF Domains 1,2,5 of human EMR2, a 7-TM immune system molecule, in complex with calcium. · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UHX3 · AlphaFold monomer V2.0 prediction for adhesion G protein-coupled receptor E2 (Q9UHX3) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q9UHX3
- Elsewhere: RCSB PDB 2BO2 · PDBe 2BO2 · UniProt Q9UHX3
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