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The soxyz complex of paracoccus pantotrophus

Analyse The soxyz complex of paracoccus pantotrophus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OXH
Type
protein
Length
878 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Soxz protein; Soxy protein
UniProt
Q9LCU8, Q9LCU9
Pockets
8 · best druggability 0.74

Structure

x-ray diffraction · 5 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Z, A, C, ESoxz proteinprotein1070% helix, 55% strandQ9LCU8
YSoxy proteinprotein1119% helix, 51% strandQ9LCU9
BSoxy proteinprotein1158% helix, 47% strandQ9LCU9
DSoxy proteinprotein1109% helix, 52% strandQ9LCU9
FSoxy proteinprotein1148% helix, 47% strandQ9LCU9

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 6 copies · chains Y, Z, A, B, D, F, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17600.740.80102EDO
21570.580.8331empty
32940.550.7648EDO
41770.540.7929empty
51800.520.7822empty

Interfaces

14 interfaces between chains.

  • C–D · 1216 Ų buried · 31 hydrogen bonds · protein-protein
  • Z–Y · 1209 Ų buried · 29 hydrogen bonds · protein-protein
  • A–B · 1144 Ų buried · 31 hydrogen bonds · protein-protein
  • E–F · 1119 Ų buried · 29 hydrogen bonds · protein-protein
  • Y–B · 610 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

  • 2OXH · The SOXYZ Complex of Paracoccus Pantotrophus · the same entry in another collection · chain Z against Z, TM-score 1.00

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