Research workbench
Crystal structure of a designed cyanovirin-N homolog lectin; lkamg in P21 space group
Analyse Crystal structure of a designed cyanovirin-N homolog lectin; lkamg in P21 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HNU
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanovirin-N-like protein
- UniProt
- Q5MK11, Q7S6U4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Cyanovirin-N-like protein | protein | 106 | 13% helix, 58% strand | Q5MK11, Q7S6U4 |
Compared structures
- 3HNU · Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG in P21 space group · the same entry in another collection · chain X against X, TM-score 1.00
- Q7S6U4 · AlphaFold monomer V2.0 prediction for cyanovirin-N homolog (Q7S6U4) · a predicted model of the same protein · chain X against A, TM-score 0.96
- Q5MK11 · AlphaFold monomer V2.0 prediction for cyanovirin-N homolog (Q5MK11) · a predicted model of the same protein · chain X against A, TM-score 0.91
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 Q5MK11
- Every structure of UniProt Q7S6U4
- Elsewhere: RCSB PDB 3HNU · PDBe 3HNU · UniProt Q5MK11 · UniProt Q7S6U4
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