› 3bq7

X-ray diffraction
2.9Å resolution

SAM domain of Diacylglycerol Kinase delta1 (E35G)

Released:
DOI: 10.2210/pdb3bq7/pdb
PDB entry 3bq7 coloured by chain, front view.
PDB entry 3bq7 coloured by chain, side view.
PDB entry 3bq7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1.
Harada BT, Knight MJ, Imai S, Qiao F, Ramachander R, Sawaya MR, Gingery M, Sakane F, Bowie JU
Structure 16 380-7 (2008)
PMID: 18334213

Function and Biology Details

Reaction catalysed: 
ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo hexamer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diacylglycerol kinase delta Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 81 amino acids
Theoretical weight: 9.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16760 (Residues: 1141-1208; Coverage: 6%)
Gene names: DGKD, KIAA0145
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P32
Unit cell:
a: 108.079Å b: 108.079Å c: 33.513Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.25 0.29
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Regulation and functions of diacylglycerol kinases.
Shulga et al. (2011)
8 more

6 mentions without citation

Advances in chemical proteomic evaluation of lipid kinases-DAG kinases as a case study.
Ware et al. (2021)
5 more