Research workbench
C1RC1S complex
Analyse C1RC1S complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F1H
- Type
- protein
- Length
- 1,128 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C1R subcomponent; Complement C1S subcomponent
- EC
- 3.4.21.41, 3.4.21.42
- UniProt
- P00736, P09871
- Ligands
- LYS, NAG, BMA, MAN, GAL, CA, NA
- Pockets
- 17 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 2% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C1R subcomponent (EC 3.4.21.41) | protein | 291 | 2% helix, 40% strand | P00736 |
| C | Complement C1R subcomponent (EC 3.4.21.41) | protein | 286 | 2% helix, 41% strand | P00736 |
| D | Complement C1S subcomponent (EC 3.4.21.42) | protein | 275 | 3% helix, 47% strand | P09871 |
| B | Complement C1S subcomponent (EC 3.4.21.42) | protein | 276 | 3% helix, 47% strand | P09871 |
Ligands and binding sites
- LYS · Lysine · ligand · chains C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A, C, D, B
- BMA · beta-D-mannopyranose · sugar · 5 copies
- MAN · alpha-D-mannopyranose · sugar · 4 copies
- GAL · beta-D-galactopyranose · sugar · 2 copies
- CA · Calcium ion · metal · 12 copies · chains A, C, D, B
- NA · Sodium ion · metal · 6 copies · chains A, C, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 832 | 0.76 | 0.80 | 78 | empty |
| 2 | 891 | 0.73 | 0.77 | 93 | empty |
| 3 | 887 | 0.70 | 0.76 | 85 | empty |
| 4 | 216 | 0.58 | 0.79 | 39 | empty |
| 5 | 348 | 0.51 | 0.73 | 39 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1426 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1416 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 1032 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide, 6 glycan (disulfide, N-glycosylation, glycosylation).
Compared structures
- 6F1H · C1rC1s complex · the same entry in another collection · chain D against D, TM-score 1.00
- P00736 · AlphaFold monomer V2.0 prediction for complement C1R subcomponent (P00736) · a predicted model of the same protein · chain A against A, TM-score 0.70
- P09871 · AlphaFold monomer V2.0 prediction for complement C1S subcomponent (P09871) · a predicted model of the same protein · chain D against A, TM-score 0.64
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 P00736
- Every structure of UniProt P09871
- Elsewhere: RCSB PDB 6F1H · PDBe 6F1H · UniProt P00736 · UniProt P09871
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