› 7a99

X-ray diffraction
1.79Å resolution

Crystal structure of the Phe57Trp mutant of the arginine-bound form of domain 1 from TmArgBP

Released:
DOI: 10.2210/pdb7a99/pdb
Model geometry
Fit model/data
PDB entry 7a99 coloured by chain, front view.
PDB entry 7a99 coloured by chain, side view.
PDB entry 7a99 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Development of a Protein Scaffold for Arginine Sensing Generated through the Dissection of the Arginine-Binding Protein from Thermotoga maritima.
Smaldone G, Ruggiero A, Balasco N, Vitagliano L
OpenAccess logo Int J Mol Sci 21 (2020)
PMID: 33053818

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino acid ABC transporter, periplasmic amino acid-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 15.23 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZ62 (Residues: 20-115, 121-233; Coverage: 50%)
Gene name: TM_0593
Sequence domains: Bacterial extracellular solute-binding proteins, family 3

Ligands and Environments

2 bound ligands:
Ligand ARG 2 x ARG
Ligand ACT 3 x ACT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 37.48Å b: 67.217Å c: 102.411Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.178 0.233
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Retracing the evolution of a modern periplasmic binding protein.
Michel et al. (2023)
1 more

1 mention without citation

Development of a Protein Scaffold for Arginine Sensing Generated through the Dissection of the Arginine-Binding Protein from Thermotoga maritima.
Smaldone et al. (2020)