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Structure of slyd from thermus thermophilus in complex with S2 peptide

Analyse Structure of slyd from thermus thermophilus in complex with S2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ODL
Type
protein
Length
354 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase slyd; 30S ribosomal protein S2
EC
5.2.1.8
UniProt
Q5SLE7, P0A7V0
Ligands
NH2, CL
Pockets
2 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptidyl-prolyl cis-trans isomerase slyd (EC 5.2.1.8)protein15015% helix, 43% strandQ5SLE7
C30S ribosomal protein S2protein90% helix, 22% strandP0A7V0
D, E, F30S ribosomal protein S2protein150% helix, 20% strandP0A7V0

Ligands and binding sites

  • NH2 · Amino group · ion · 4 copies · chains B, C, A, D, E, F
  • CL · Chloride ion · ion · 2 copies · chains A, F, B, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11530.590.8323empty
21900.460.7420empty

Interfaces

5 interfaces between chains.

  • A–D · 828 Ų buried · 5 hydrogen bonds · protein-protein
  • A–F · 790 Ų buried · 11 hydrogen bonds · protein-protein
  • B–E · 776 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 460 Ų buried · 3 hydrogen bonds · protein-protein
  • D–F · 19 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4ODL · Structure of SlyD from Thermus thermophilus in complex with S2 peptide · the same entry in another collection · chain A against A, TM-score 1.00

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