Research workbench
Crystal structure of unliganded human CD21 SCR1-SCR2 (complement receptor type 2)
Analyse Crystal structure of unliganded human CD21 SCR1-SCR2 (complement receptor type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LY2
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement receptor type 2
- UniProt
- P20023
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement receptor type 2 | protein | 130 | 0% helix, 44% strand | P20023 |
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: 4 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 1LY2 · Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2) · the same entry in another collection · chain A against A, TM-score 1.00
- P20023 · AlphaFold monomer V2.0 prediction for complement receptor type 2 (P20023) · 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 P20023
- Elsewhere: RCSB PDB 1LY2 · PDBe 1LY2 · UniProt P20023
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.