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Mammalian clock protein MPER2 - crystal structure of a pas domain fragment

Analyse Mammalian clock protein MPER2 - crystal structure of a pas domain fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3GDI
Type
protein
Length
519 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Period circadian protein homolog 2
UniProt
O54943
Pockets
10 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeriod circadian protein homolog 2protein26920% helix, 32% strandO54943
BPeriod circadian protein homolog 2protein25021% helix, 32% strandO54943

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15990.790.8561empty
25170.770.8454empty
33020.550.7639empty
41760.530.7923empty
5650.490.8313empty

Interfaces

1 interface between chains.

  • A–B · 1344 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3GDI · Mammalian Clock Protein mPER2 - Crystal Structure of a PAS Domain Fragment · the same entry in another collection · chain A against A, TM-score 1.00
  • O54943 · AlphaFold monomer V2.0 prediction for period circadian protein homolog 2 (O54943) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

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