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Crystal structure of the peptidyl-prolyl cis-trans isomerase (ppib) from streptococcus pyogenes.

Analyse Crystal structure of the peptidyl-prolyl cis-trans isomerase (ppib) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L6Y
Type
protein
Length
418 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase
EC
5.2.1.8
UniProt
Q1JI83
Pockets
8 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein20922% helix, 24% strandQ1JI83

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.660.8236empty
21060.340.7319empty
3640.330.7720empty
4800.330.7414empty
5760.320.7414empty

Interfaces

1 interface between chains.

  • A–B · 421 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 7L6Y · Crystal Structure of the Peptidyl-Prolyl Cis-Trans Isomerase (PpiB) from Streptococcus… · the same entry in another collection · chain A against A, TM-score 1.00

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