Research workbench
1.9 ångström crystal structure of CLEC5A
Analyse 1.9 ångström crystal structure of CLEC5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YHF
- Type
- protein
- Length
- 1,062 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-type lectin domain family 5 member a
- UniProt
- Q9NY25
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | C-type lectin domain family 5 member a | protein | 118 | 17% helix, 36% strand | Q9NY25 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1165 | 0.79 | 0.81 | 115 | empty |
| 2 | 1159 | 0.76 | 0.79 | 118 | empty |
| 3 | 88 | 0.62 | 0.90 | 24 | empty |
| 4 | 169 | 0.59 | 0.83 | 28 | empty |
| 5 | 228 | 0.57 | 0.79 | 24 | empty |
Interfaces
17 interfaces between chains.
- A–F · 872 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 864 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 576 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 556 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 555 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 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 Q9NY25
- Elsewhere: RCSB PDB 2YHF · PDBe 2YHF · UniProt Q9NY25
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