Research workbench
Crystal structure of the catalytic domain of human complement C1S protease
Analyse Crystal structure of the catalytic domain of human complement C1S protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ELV
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C1S component
- EC
- 3.4.21.42
- UniProt
- P09871
- Ligands
- NES, NAG, FUC, SO4
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C1S component (EC 3.4.21.42) | protein | 303 | 10% helix, 35% strand | P09871 |
Ligands and binding sites
- NES · 2-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-ethanesulfonic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
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 | 171 | 0.51 | 0.78 | 33 | SO4 |
| 2 | 152 | 0.41 | 0.74 | 29 | empty |
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1ELV · Crystal structure of the catalytic domain of human complement C1S protease · the same entry in another collection · chain A against A, TM-score 1.00
- P09871 · AlphaFold monomer V2.0 prediction for complement C1S subcomponent (P09871) · a predicted model of the same protein · chain A 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 P09871
- Elsewhere: RCSB PDB 1ELV · PDBe 1ELV · UniProt P09871
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