› 3tda

X-ray diffraction
2.67Å resolution

Competitive replacement of thioridazine by prinomastat in crystals of cytochrome P450 2D6

Released:
DOI: 10.2210/pdb3tda/pdb
PDB entry 3tda coloured by chain, front view.
PDB entry 3tda coloured by chain, side view.
PDB entry 3tda coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contributions of ionic interactions and protein dynamics to cytochrome P450 2D6 (CYP2D6) substrate and inhibitor binding.
Wang A, Stout CD, Zhang Q, Johnson EF
J Biol Chem 290 5092-5104 (2015)
PMID: 25555909

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 2D6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 479 amino acids
Theoretical weight: 53.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P10635 (Residues: 34-497; Coverage: 93%)
Gene names: CYP2D6, CYP2DL1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

3 bound ligands:
Ligand HEM 4 x HEM
Ligand PN0 4 x PN0
Ligand ZN 5 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 57.05Å b: 192.74Å c: 247.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.255
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

7 review citations

Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs.
Jabłońska-Trypuć et al. (2016)
6 more

13 mentions without citation

Polymorphic cytochrome P450 enzymes (CYPs) and their role in personalized therapy.
Preissner et al. (2013)
12 more