Research workbench
Crystal structure of C1QL1
Analyse Crystal structure of C1QL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QQ2
- Type
- protein
- Length
- 392 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C1Q-related factor
- UniProt
- O88992
- Ligands
- CD
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | C1Q-related factor | protein | 131 | 0% helix, 56% strand | O88992 |
| C | C1Q-related factor | protein | 130 | 0% helix, 59% strand | O88992 |
Ligands and binding sites
- CD · Cadmium ion · metal · 18 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.73 | 0.99 | 14 | CD |
| 2 | 116 | 0.44 | 0.77 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1088 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1055 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 1023 Ų buried · 20 hydrogen bonds · protein-protein
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 O88992
- Elsewhere: RCSB PDB 4QQ2 · PDBe 4QQ2 · UniProt O88992
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