Research workbench
Complement component C2A
Analyse Complement component C2A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I6S
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C2A fragment
- EC
- 3.4.21.43
- UniProt
- P06681
- Ligands
- NAG, BMA, FUL
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C2A fragment (EC 3.4.21.43) | protein | 497 | 30% helix, 24% strand | P06681 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies
- FUL · beta-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.52 | 0.84 | 18 | empty |
| 2 | 74 | 0.48 | 0.84 | 20 | NAG |
| 3 | 115 | 0.39 | 0.76 | 22 | empty |
| 4 | 77 | 0.30 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 5 disulfide, 5 glycan (disulfide, N-glycosylation).
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 P06681
- Elsewhere: RCSB PDB 2I6S · PDBe 2I6S · UniProt P06681
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