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Thermostable thymidylate synthase a from bacillus subtilis

Analyse Thermostable thymidylate synthase a from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BKO
Type
protein
Length
1,112 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thymidylate synthase a
EC
2.1.1.45
UniProt
P42326
Pockets
6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DThymidylate synthase a (EC 2.1.1.45)protein27830% helix, 25% strandP42326

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18240.760.8080empty
28480.750.7983empty
37710.740.7966empty
47460.720.7869empty
5780.510.8418empty

Interfaces

2 interfaces between chains.

  • A–B · 2414 Ų buried · 46 hydrogen bonds · protein-protein
  • C–D · 2336 Ų buried · 47 hydrogen bonds · protein-protein

Compared structures

  • 1BKO · Thermostable thymidylate synthase a from bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00

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