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3.10 ångström resolution crystal structure of foldase protein (prsa) from lactococcus lactis

Analyse 3.10 ångström resolution crystal structure of foldase protein (prsa) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VJ2
Type
protein
Length
1,080 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Foldase
EC
5.2.1.8
UniProt
Q9CEV9
Pockets
11 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 59% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFoldase (EC 5.2.1.8)protein27159% helix, 14% strandQ9CEV9
BFoldase (EC 5.2.1.8)protein27059% helix, 14% strandQ9CEV9
CFoldase (EC 5.2.1.8)protein26959% helix, 14% strandQ9CEV9
DFoldase (EC 5.2.1.8)protein27059% helix, 14% strandQ9CEV9

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18420.700.7679empty
27970.670.7481empty
37030.660.7576empty
43580.550.7441empty
52070.540.7833empty

Interfaces

6 interfaces between chains.

  • A–B · 1551 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 1352 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 697 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 687 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 106 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

  • 6VJ2 · 3.10 Angstrom Resolution Crystal Structure of Foldase Protein (PrsA) from Lactococcus… · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9CEV9 · AlphaFold monomer V2.0 prediction for foldase protein prsa (Q9CEV9) · a predicted model of the same protein · chain D against A, TM-score 0.95

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