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Solution NMR structure of complex of 1:2 cyanovirin-N:MAN-ALPHA1,2- man-alpha restrained regularized mean coordinates
Analyse Solution NMR structure of complex of 1:2 cyanovirin-N:MAN-ALPHA1,2- man-alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IIY
- Type
- protein
- Length
- 101 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanovirin-N
- UniProt
- P81180
- Ligands
- MAN
Structure
solution nmr · 1 distinct chain · 13% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyanovirin-N | protein | 101 | 13% helix, 57% strand | P81180 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1IIY · Solution NMR Structure of Complex of 1:2 Cyanovirin-N:Man-Alpha1,2-Man-Alpha Restrained… · the same entry in another collection · chain A against A, TM-score 1.00
- P81180 · AlphaFold monomer V2.0 prediction for cyanovirin-N (P81180) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P81180
- Elsewhere: RCSB PDB 1IIY · PDBe 1IIY · UniProt P81180
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