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MolNFT v1 · #102163 · protein

Structure of slyd from thermus thermophilus in complex with T1 peptide

4ODK · Peptidyl-prolyl cis-trans isomerase slyd: “Structure of slyd from thermus thermophilus in complex with T1 peptide”. X-ray diffraction, 2 ligands (NH2, CL), 1 pocket (best druggability 0.29). MolNFT v1 #102163 on GenesisL1: 3D…

PDB
4ODK
Type
protein
Length
164 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase slyd; Guanyl-specific ribonuclease T1
EC
5.2.1.8
UniProt
Q5SLE7, P00651
Ligands
NH2, CL
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase slyd (EC 5.2.1.8)protein15314% helix, 45% strandQ5SLE7
BGuanyl-specific ribonuclease T1protein80% helix, 13% strandP00651
CGuanyl-specific ribonuclease T1protein30% helix, 0% strandP00651

Ligands and binding sites

  • NH2 · Amino group · ion · chains A, B
  • CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.290.7517CL

Interfaces

2 interfaces between chains.

  • A–B · 457 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 369 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 4ODK · Structure of SlyD from Thermus thermophilus in complex with T1 peptide · the same entry in another collection · chain A against A, TM-score 1.00

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