› 3hbz

X-ray diffraction
2.05Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative carbohydrate metabolism domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 37.66 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A605 (Residues: 21-361; Coverage: 95%)
Gene name: BT_2081
Sequence domains: Putative carbohydrate metabolism domain
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand CAC 2 x CAC
Ligand ACT 2 x ACT
Ligand PEG 12 x PEG
Ligand P6G 7 x P6G
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P3221
Unit cell:
a: 94.551Å b: 94.551Å c: 107.812Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.159 0.191
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.
Fleischman et al. (2014)

1 mention without citation

Structure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: the first structural representative of a new protein family that may play a role in carbohydrate metabolism.
Yeh et al. (2010)