› 3aof

X-ray diffraction
1.29Å resolution

Crystal structures of Thermotoga maritima Cel5A in complex with Mannotriose substrate

Released:
DOI: 10.2210/pdb3aof/pdb
PDB entry 3aof coloured by chain, front view.
PDB entry 3aof coloured by chain, side view.
PDB entry 3aof coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.
Wu TH, Huang CH, Ko TP, Lai HL, Ma Y, Chen CC, Cheng YS, Liu JR, Guo RT
Biochim Biophys Acta 1814 1832-40 (2011)
PMID: 21839861

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194874 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glycoside hydrolase family 5 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 37.31 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X273 (Residues: 1-317; Coverage: 100%)
Gene name: TM_1751
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: BMA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21
Unit cell:
a: 62.696Å b: 77.946Å c: 62.959Å
α: 90° β: 97.16° γ: 90°
R-values:
R R work R free
0.173 0.172 0.188
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Weaving of bacterial cellulose by the Bcs secretion systems.
Abidi et al. (2022)
1 more

4 mentions without citation

Kinetic and structural analysis for potent antifolate inhibition of Pneumocystis jirovecii, Pneumocystis carinii, and human dihydrofolate reductases and their active-site variants.
Cody et al. (2013)
3 more