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Thiobacillus denitrificans bph

Analyse Thiobacillus denitrificans bph in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OVS
Type
protein
Length
2,593 residues
Chains
14
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bph
Pockets
20 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, L, M, NBphprotein18530% helix, 31% strand—
JBphprotein18630% helix, 30% strand—
KBphprotein18729% helix, 29% strand—

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17100.710.7898empty
22870.580.7858empty
32280.570.7934empty
42060.560.7930empty
52400.550.7833empty

Interfaces

28 interfaces between chains.

  • B–C · 1202 Ų buried · 22 hydrogen bonds · protein-protein
  • E–F · 1201 Ų buried · 20 hydrogen bonds · protein-protein
  • D–E · 1201 Ų buried · 25 hydrogen bonds · protein-protein
  • M–N · 1200 Ų buried · 24 hydrogen bonds · protein-protein
  • H–N · 1198 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 5OVS · Thiobacillus denitrificans BPH · the same entry in another collection · chain A against A, TM-score 1.00

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