› 5c2n

X-ray diffraction
1.65Å resolution

The de novo evolutionary emergence of a symmetrical protein is shaped by folding constraints

Released:
DOI: 10.2210/pdb5c2n/pdb
PDB entry 5c2n coloured by chain, front view.
PDB entry 5c2n coloured by chain, side view.
PDB entry 5c2n coloured by chain, top view.
Source organism: Enterobacteria phage L1
Primary publication:
De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.
Smock RG, Yadid I, Dym O, Clarke J, Tawfik DS
Cell 164 476-86 (2016)
PMID: 26806127

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tachylectin 2 domain-containing protein Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 48 amino acids
Theoretical weight: 5.31 KDa
Source organism: Enterobacteria phage L1
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A140UHM9 (Residues: 1-48; Coverage: 100%)
Sequence domains: Tachylectin

Ligands and Environments

1 bound ligand:
Ligand NAG 15 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3112
Unit cell:
a: 112.219Å b: 112.219Å c: 107.29Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.186 0.248
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Computational design of protein self-assembly.
Norn et al. (2016)
6 more

1 mention without citation

Mechanisms of protein evolution.
Jayaraman et al. (2022)