› 1ln2

X-ray diffraction
2.9Å resolution

Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine (Seleno-Met Protein)

Released:
DOI: 10.2210/pdb1ln2/pdb
PDB 1ln2 coloured by chain and viewed from the front.
PDB 1ln2 coloured by chain and viewed from the side.
PDB 1ln2 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structure of human phosphatidylcholine transfer protein in complex with its ligand.
Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE
Nat. Struct. Biol. 9 507-11 (2002)
PMID: 12055623

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylcholine transfer protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 25.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UKL6 (Residues: 1-214; Coverage: 100%)
Gene names: PCTP, STARD2
Sequence domains: START domain
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

1 bound ligand:
Ligand DLP 2 x DLP
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P4212
Unit cell:
a: 134.7Å b: 134.7Å c: 82.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.231 0.293
Expression system: Escherichia coli

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Citations

28 review citations

Florigen and its homologs of FT/CETS/PEBP/RKIP/YbhB family may be the enzymes of small molecule metabolism: review of the evidence.
Tsoy et al. (2022)
27 more

5 mentions without citation

Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.
Guest et al. (2018)
4 more