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Crystal structure of ppic-type peptidyl-prolyl cis-trans isomerase domain at 1.55A resolution.

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

PDB
3GPK
Type
protein
Length
216 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ppic-type peptidyl-prolyl cis-trans isomerase
EC
5.2.1.8
UniProt
Q2G9Z0
Ligands
SO4
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APpic-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein10842% helix, 31% strandQ2G9Z0
BPpic-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)protein10838% helix, 31% strandQ2G9Z0

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.590.8126empty

Interfaces

1 interface between chains.

  • A–B · 441 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 3GPK · Crystal Structure of PpiC-type peptidyl-prolyl cis-trans isomerase domain at 1.55A… · the same entry in another collection · chain A against A, TM-score 1.00

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