› 3hnu

X-ray diffraction
1.56Å resolution

Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG in P21 space group

Released:
DOI: 10.2210/pdb3hnu/pdb
PDB entry 3hnu coloured by chain, front view.
PDB entry 3hnu coloured by chain, side view.
PDB entry 3hnu coloured by chain, top view.
Source organisms:
Primary publication:
A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.
Koharudin LM, Furey W, Gronenborn AM
Proteins 77 904-15 (2009)
PMID: 19639634

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyanovirin-N homolog Chain: X
Molecule details ›
Chain: X
Length: 110 amino acids
Theoretical weight: 12.39 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q7S6U4 (Residues: 1-2, 42-96; Coverage: 51%)
  • Canonical: Q5MK11 (Residues: 3-39, 91-103; Coverage: 49%)
Gene name: NCU05495
Sequence domains: CVNH domain
Structure domains: Cyanovirin-N

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 33.876Å b: 34.444Å c: 45.632Å
α: 90° β: 101.24° γ: 90°
R-values:
R R work R free
0.187 0.183 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Carbohydrate-protein interactions: a 3D view by NMR.
Roldós et al. (2011)
1 more

1 mention without citation

A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.
Koharudin et al. (2009)