Research workbench
Mouse scavenger receptor C-type lectin carbohydrate-recognition domain.
Analyse Mouse scavenger receptor C-type lectin carbohydrate-recognition domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OX9
- Type
- protein
- Length
- 518 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collectin placenta 1
- UniProt
- Q8K4Q8
- Ligands
- NAG, FUC, GAL, CA
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Collectin placenta 1 | protein | 130 | 17% helix, 28% strand | Q8K4Q8 |
| B | Collectin placenta 1 | protein | 127 | 19% helix, 29% strand | Q8K4Q8 |
| C | Collectin placenta 1 | protein | 131 | 18% helix, 28% strand | Q8K4Q8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains C
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B, C, D
- GAL · beta-D-galactopyranose · sugar · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 16 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.81 | 0.83 | 84 | NAG, FUC |
| 2 | 196 | 0.51 | 0.77 | 34 | empty |
| 3 | 103 | 0.38 | 0.75 | 20 | empty |
| 4 | 86 | 0.35 | 0.75 | 23 | empty |
Interfaces
4 interfaces between chains.
- A–C · 533 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 470 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 461 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 188 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 Q8K4Q8
- Elsewhere: RCSB PDB 2OX9 · PDBe 2OX9 · UniProt Q8K4Q8
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