› 1ytv

X-ray diffraction
1.8Å resolution

Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor

Released:
DOI: 10.2210/pdb1ytv/pdb
PDB entry 1ytv coloured by chain, front view.
PDB entry 1ytv coloured by chain, side view.
PDB entry 1ytv coloured by chain, top view.
Source organisms:
Primary publication:
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M
Acta Crystallogr Sect F Struct Biol Cryst Commun 61 341-5 (2005)
PMID: 16511036

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142638 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Maltose/maltodextrin-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 40.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II
Vasopressin V1a receptor Chains: M, N
Molecule details ›
Chains: M, N
Length: 84 amino acids
Theoretical weight: 9.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P37288 (Residues: 361-361, 362-418; Coverage: 14%)
Gene names: AVPR1, AVPR1A
Sequence domains: Vasopressin V1 receptor, C-terminal

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 51.102Å b: 66.557Å c: 115.723Å
α: 90° β: 95.99° γ: 90°
R-values:
R R work R free
0.196 0.199 0.225
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Site-specific protein modification through Cu(I)-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication.
Lin et al. (2006)
3 more

9 mentions without citation

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
8 more