› 1ov2

Solution NMR

Ensemble of the solution structures of domain one of receptor associated protein

Released:
DOI: 10.2210/pdb1ov2/pdb
PDB entry 1ov2 coloured by chain, ensemble of 39 models, front view.
PDB entry 1ov2 coloured by chain, ensemble of 39 models, side view.
PDB entry 1ov2 coloured by chain, ensemble of 39 models, top view.
Source organism: Homo sapiens
Primary publication:
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein.
Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX
J Biomol NMR 26 187-8 (2003)
PMID: 12766414

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-2-macroglobulin receptor-associated protein Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30533 (Residues: 35-133; Coverage: 31%)
Gene names: A2MRAP, LRPAP1
Sequence domains: Alpha-2-macroglobulin RAP, N-terminal domain
Structure domains: RAP domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsiona angle dynamics and simulated anealing
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The structure of receptor-associated protein (RAP).
Lee et al. (2007)
3 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)