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Streptococcus suis sadp mutant - N285D

Analyse Streptococcus suis sadp mutant - N285D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YRO
Type
protein
Length
1,020 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sadp
UniProt
G5DSS1
Ligands
NA
Pockets
5 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D, A, B, C, ESadpprotein20417% helix, 43% strandG5DSS1

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, C, E
  • GOL · Glycerol · additive · 7 copies · chains D, B, A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13630.550.7450empty
2880.440.8022empty
3580.440.8321empty
4730.390.7822GOL
5580.350.7815empty

Interfaces

5 interfaces between chains.

  • A–C · 412 Ų buried · 6 hydrogen bonds · protein-protein
  • D–B · 402 Ų buried · 7 hydrogen bonds · protein-protein
  • C–E · 195 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 97 Ų buried · 1 hydrogen bond · protein-protein
  • D–A · 96 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6YRO · Streptococcus suis SadP mutant - N285D · the same entry in another collection · chain D against D, TM-score 1.00

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