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Apo crystal structure of octaketide synthase from a. arborescens

Analyse Apo crystal structure of octaketide synthase from a. arborescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DTQ
Type
protein
Length
1,560 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Octaketide synthase 1
EC
2.3.1.-
UniProt
Q3L7F5
Pockets
11 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DOctaketide synthase 1 (EC 2.3.1.-)protein39044% helix, 24% strandQ3L7F5

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15780.770.8462empty
23500.760.8659empty
33440.750.8650empty
43030.740.8653empty
52910.560.7635empty

Interfaces

3 interfaces between chains.

  • A–B · 3132 Ų buried · 79 hydrogen bonds · protein-protein
  • A–C · 363 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 178 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 7DTQ · Apo Crystal Structure of Octaketide Synthase from A. arborescens · the same entry in another collection · chain A against A, TM-score 1.00
  • Q3L7F5 · AlphaFold monomer V2.0 prediction for octaketide synthase 1 (Q3L7F5) · a predicted model of the same protein · chain A against A, TM-score 1.00

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