› 7fiq

X-ray diffraction
2.22Å resolution

The crystal structure of mannose-bound beta-1,2-mannobiose phosphorylase from Thermoanaerobacter sp.

Released:
DOI: 10.2210/pdb7fiq/pdb
Model geometry
Fit model/data
PDB entry 7fiq coloured by chain, front view.
PDB entry 7fiq coloured by chain, side view.
PDB entry 7fiq coloured by chain, top view.
Source organism: Thermoanaerobacter sp. X514
Primary publication:
Structural investigation of a thermostable 1,2-β-mannobiose phosphorylase from Thermoanaerobacter sp. X-514.
Dai L, Chang Z, Yang J, Liu W, Yang Y, Chen CC, Zhang L, Huang JW, Sun Y, Guo RT
Biochem Biophys Res Commun 579 54-61 (2021)
PMID: 34587555

Function and Biology Details

Reaction catalysed: 
Beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate = D-mannopyranose + alpha-D-mannose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-1,2-mannobiose phosphorylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 313 amino acids
Theoretical weight: 35.86 KDa
Source organism: Thermoanaerobacter sp. X514
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B0K2C3 (Residues: 1-302; Coverage: 100%)
Gene name: Teth514_1789
Sequence domains: beta-1,4-mannooligosaccharide phosphorylase

Ligands and Environments

5 bound ligands:
Ligand MAN 4 x MAN
Ligand GOL 1 x GOL
Ligand PGE 2 x PGE
Ligand ZN 17 x ZN
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER METALJET
Spacegroup: I4
Unit cell:
a: 203.195Å b: 203.195Å c: 77.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.22
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.
Li et al. (2022)
1 more