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X-ray diffraction
2.07Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-564131 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tripartite tricarboxylate transporter substrate binding protein Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 35.72 KDa
Source organism: Rhodopseudomonas palustris CGA009
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6N193 (Residues: 37-335; Coverage: 100%)
Gene names: RPA4515, TX73_023445
Sequence domains: Tripartite tricarboxylate transporter family receptor

Ligands and Environments

4 bound ligands:
Ligand 0L1 1 x 0L1
Ligand SO4 3 x SO4
Ligand GOL 2 x GOL
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 46.9Å b: 166.609Å c: 82.175Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.254
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity.
Rosa et al. (2018)
1 more

1 mention without citation

Structural basis for high-affinity adipate binding to AdpC (RPA4515), an orphan periplasmic-binding protein from the tripartite tricarboxylate transporter (TTT) family in Rhodopseudomonas palustris.
Rosa et al. (2017)