› 1beh

X-ray diffraction
1.75Å resolution

HUMAN PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN IN COMPLEX WITH CACODYLATE

Released:
DOI: 10.2210/pdb1beh/pdb
PDB entry 1beh coloured by chain, front view.
PDB entry 1beh coloured by chain, side view.
PDB entry 1beh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction.
Banfield MJ, Barker JJ, Perry AC, Brady RL
Structure 6 1245-54 (1998)
PMID: 9782050

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylethanolamine-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 187 amino acids
Theoretical weight: 21.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P30086 (Residues: 1-187; Coverage: 100%)
Gene names: PBP, PEBP, PEBP1
Sequence domains: Phosphatidylethanolamine-binding protein
Structure domains: PEBP-like

Ligands and Environments

1 bound ligand:
Ligand CAC 2 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 45.43Å b: 61.63Å c: 67.92Å
α: 90° β: 101.09° γ: 90°
R-values:
R R work R free
0.235 0.235 0.286
Expression system: Escherichia coli BL21

Quick links

Citations

23 review citations

Environmental-dependent acceleration of a developmental switch: the floral transition.
Simpson et al. (2000)
22 more

13 mentions without citation

PEBP1 Wardens Ferroptosis by Enabling Lipoxygenase Generation of Lipid Death Signals.
Wenzel et al. (2017)
12 more