Research workbench
Crystal structure of dc-sign carbohydrate recognition domain complexed with MAN4
Analyse Crystal structure of dc-sign carbohydrate recognition domain complexed with MAN4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SL4
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mdc-SIGN1B type I isoform
- Ligands
- MAN, CA
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mdc-SIGN1B type I isoform | protein | 132 | 20% helix, 30% strand | — |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · 3 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 (disulfide).
Compared structures
- 1SL4 · Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with Man4 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1SL4 · PDBe 1SL4
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