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Crystal structure of protein with a cyclophilin-like fold (YP_831253.1) from arthrobacter sp. FB24 at 1.90 a resolution

Analyse Crystal structure of protein with a cyclophilin-like fold (YP_831253.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KOP
Type
protein
Length
971 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein
UniProt
A0JVT3
Pockets
7 · best druggability 0.71

Structure

x-ray diffraction · 6 distinct chains · 19% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized proteinprotein15820% helix, 40% strandA0JVT3
BUncharacterized proteinprotein15618% helix, 40% strandA0JVT3
CUncharacterized proteinprotein16517% helix, 39% strandA0JVT3
DUncharacterized proteinprotein15818% helix, 40% strandA0JVT3
EUncharacterized proteinprotein16517% helix, 38% strandA0JVT3
FUncharacterized proteinprotein16926% helix, 37% strandA0JVT3

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18230.710.77120empty
25100.650.7786empty
35550.610.7465empty
42670.510.7451empty
51050.370.7424empty

Interfaces

12 interfaces between chains.

  • C–E · 1432 Ų buried · 44 hydrogen bonds · protein-protein
  • A–B · 1369 Ų buried · 45 hydrogen bonds · protein-protein
  • D–F · 1305 Ų buried · 38 hydrogen bonds · protein-protein
  • B–E · 492 Ų buried · 14 hydrogen bonds · protein-protein
  • C–F · 490 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 3KOP · Crystal structure of Protein with a cyclophilin-like fold (YP_831253.1) from Arthrobacter… · the same entry in another collection · chain A against A, TM-score 1.00

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