› 4b16

X-ray diffraction
1.61Å resolution

crystal structure of tamarind chitinase like lectin (TCLL) complexed with N-acetyl glucosamine (GlcNAc)

Released:
DOI: 10.2210/pdb4b16/pdb
PDB entry 4b16 coloured by chain, front view.
PDB entry 4b16 coloured by chain, side view.
PDB entry 4b16 coloured by chain, top view.
Source organism: Tamarindus indica
Primary publication:
Structural investigation of a novel N-acetyl glucosamine binding chi-lectin which reveals evolutionary relationship with class III chitinases.
Patil DN, Datta M, Dev A, Dhindwal S, Singh N, Dasauni P, Kundu S, Sharma AK, Tomar S, Kumar P
PLoS One 8 e63779 (2013)
PMID: 23717482

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197414 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
GH18 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.93 KDa
Source organism: Tamarindus indica
UniProt:
  • Canonical: S4S1V9 (Residues: 1-266; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 18
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
5 bound ligands:
Ligand GOL 1 x GOL
Ligand ACT 1 x ACT
Ligand NAG 2 x NAG
Ligand MPD 1 x MPD
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR-H
Spacegroup: P43212
Unit cell:
a: 100.061Å b: 100.061Å c: 81.843Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.182

Quick links

Citations

8 citation in other articles

Glycan complexity dictates microbial resource allocation in the large intestine.
Rogowski et al. (2015)
7 more

3 mentions without citation

Research advances and prospects of legume lectins.
Katoch et al. (2021)
2 more