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Crystal structure of human CD226
Analyse Crystal structure of human CD226 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ISB
- Type
- protein
- Length
- 544 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CD226 antigen
- UniProt
- Q15762
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CD226 antigen | protein | 221 | 5% helix, 48% strand | Q15762 |
| B | CD226 antigen | protein | 218 | 7% helix, 48% strand | Q15762 |
| C | CD226 antigen | protein | 105 | 6% helix, 49% strand | Q15762 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1172 | 0.81 | 0.82 | 107 | empty |
| 2 | 57 | 0.38 | 0.80 | 22 | empty |
| 3 | 95 | 0.36 | 0.75 | 21 | empty |
| 4 | 73 | 0.32 | 0.74 | 14 | empty |
| 5 | 54 | 0.30 | 0.75 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 910 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 784 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 484 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
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 Q15762
- Elsewhere: RCSB PDB 6ISB · PDBe 6ISB · UniProt Q15762
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