Research workbench
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
Analyse Structure of a soluble, glycosylated form of the human complement regulatory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CDS
- Type
- protein
- Length
- 77 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CD59
- UniProt
- P13987
- Ligands
- NAG
Structure
solution nmr · 1 distinct chain · 6% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CD59 | protein | 77 | 6% helix, 30% strand | P13987 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1CDS · Structure of a soluble, glycosylated form of the human complement regulatory protein CD59 · the same entry in another collection · chain A against A, TM-score 1.00
- P13987 · AlphaFold monomer V2.0 prediction for CD59 glycoprotein (P13987) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P13987
- Elsewhere: RCSB PDB 1CDS · PDBe 1CDS · UniProt P13987
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