› 2gyt

Solution NMR

Solution structure of the SAM (sterile alpha motif) domain of DLC1 (deleted in liver cancer 1)

Released:
DOI: 10.2210/pdb2gyt/pdb
PDB entry 2gyt coloured by chain, ensemble of 10 models, front view.
PDB entry 2gyt coloured by chain, ensemble of 10 models, side view.
PDB entry 2gyt coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration.
Zhong D, Zhang J, Yang S, Soh UJ, Buschdorf JP, Zhou YT, Yang D, Low BC
J Cell Sci 122 414-24 (2009)
PMID: 19158340

Function and Biology Details

Biochemical function:
  • not assigned
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-188693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rho GTPase-activating protein 7 Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96QB1 (Residues: 449-513; Coverage: 4%)
Gene names: ARHGAP7, DLC1, KIAA1723, STARD12
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Rho regulation: DLC proteins in space and time.
Braun et al. (2015)
4 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)