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Crystal structure of proteus mirabilis scsc in a transitional conformation

Analyse Crystal structure of proteus mirabilis scsc in a transitional conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IDR
Type
protein
Length
1,315 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dsba-like protein
UniProt
C2LPE2
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 5 distinct chains · 59% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDsba-like proteinprotein21961% helix, 11% strandC2LPE2
CDsba-like proteinprotein21659% helix, 12% strandC2LPE2
DDsba-like proteinprotein22160% helix, 10% strandC2LPE2
EDsba-like proteinprotein22156% helix, 12% strandC2LPE2
FDsba-like proteinprotein21958% helix, 11% strandC2LPE2

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15100.850.9254empty
27940.850.8893empty
34920.780.8665empty
41190.770.9622empty
51210.630.8722empty

Interfaces

12 interfaces between chains.

  • E–F · 2076 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 1959 Ų buried · 23 hydrogen bonds · protein-protein
  • D–E · 1613 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1553 Ų buried · 20 hydrogen bonds · protein-protein
  • D–F · 1019 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 5IDR · Crystal structure of Proteus Mirabilis ScsC in a transitional conformation · the same entry in another collection · chain A against A, TM-score 1.00

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