› 2kap

Solution NMR

Solution structure of DLC1-SAM

Released:
DOI: 10.2210/pdb2kap/pdb
PDB entry 2kap coloured by chain, ensemble of 10 models, front view.
PDB entry 2kap coloured by chain, ensemble of 10 models, side view.
PDB entry 2kap coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level.
Yang S, Noble CG, Yang D
Biochemistry 48 4040-9 (2009)
PMID: 19317456

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-188693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rho GTPase-activating protein 7 Chain: A
Molecule details ›
Chain: A
Length: 60 amino acids
Theoretical weight: 7.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96QB1 (Residues: 454-513; 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 citation in other articles

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Gao et al. (2013)
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)