Research workbench
High resolution structure of complement C1Q-like protein 3 C1Q domain
Analyse High resolution structure of complement C1Q-like protein 3 C1Q domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YBZ
- Type
- protein
- Length
- 405 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9ESN4
- Ligands
- NA, CA, SO4, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 136 | — | Q9ESN4 |
| C | — | protein | 133 | — | Q9ESN4 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, C, D
- CA · Calcium ion · metal · chains A, C, D
- SO4 · Sulfate ion · ion · 8 copies · chains A, D, C
- CL · Chloride ion · ion · chains A, C
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YBZ · High resolution structure of complement C1q-like protein 3 C1q domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ESN4 · AlphaFold monomer V2.0 prediction for complement C1Q-like protein 3 (Q9ESN4) · a predicted model of the same protein · chain D against A, TM-score 0.98
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 Q9ESN4
- Elsewhere: RCSB PDB 5YBZ · PDBe 5YBZ · UniProt Q9ESN4
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