Research workbench
Human complement C4
Analyse Human complement C4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FXK
- Type
- protein
- Length
- 1,638 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C4 beta chain; Complement C4-a alpha chain; Complement C4 gamma chain
- UniProt
- P0C0L4
- Ligands
- NAG, BMA
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C4 beta chain | protein | 651 | 6% helix, 44% strand | P0C0L4 |
| B | Complement C4-a alpha chain | protein | 697 | 31% helix, 22% strand | P0C0L4 |
| C | Complement C4 gamma chain | protein | 290 | 14% helix, 34% strand | P0C0L4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains B, C, A
- BMA · beta-D-mannopyranose · sugar · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.72 | 0.88 | 27 | empty |
| 2 | 164 | 0.72 | 0.90 | 31 | empty |
| 3 | 579 | 0.72 | 0.80 | 63 | empty |
| 4 | 371 | 0.71 | 0.84 | 34 | empty |
| 5 | 679 | 0.71 | 0.78 | 54 | empty |
Interfaces
3 interfaces between chains.
- B–C · 4514 Ų buried · 53 hydrogen bonds · protein-protein
- A–B · 4184 Ų buried · 58 hydrogen bonds · protein-protein
- A–C · 130 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- P0C0L4 · AlphaFold monomer V2.0 prediction for complement C4-a (P0C0L4) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P0C0L4
- Elsewhere: RCSB PDB 4FXK · PDBe 4FXK · UniProt P0C0L4
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