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Three-dimensional structure of the C65A-W54F double mutant of human lipocalin-type prostaglandin D synthase apo-form

Analyse Three-dimensional structure of the C65A-W54F double mutant of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OS0
Type
protein
Length
326 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Prostaglandin-H2 D-isomerase
EC
5.3.99.2
UniProt
P41222
Pockets
3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProstaglandin-H2 D-isomerase (EC 5.3.99.2)protein16312% helix, 44% strandP41222

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15410.710.7937empty
23650.710.8234empty
31040.410.7723empty

Interfaces

1 interface between chains.

  • A–B · 569 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4OS0 · Three-dimensional structure of the C65A-W54F double mutant of Human lipocalin-type… · the same entry in another collection · chain A against A, TM-score 1.00
  • P41222 · AlphaFold monomer V2.0 prediction for prostaglandin-H2 D-isomerase (P41222) · a predicted model of the same protein · chain A against A, TM-score 0.95

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