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Crystal structure of the protein Q88SR8 from lactobacillus plantarum. northeast structural genomics consortium target LPR109.

Analyse Crystal structure of the protein Q88SR8 from lactobacillus plantarum. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DC7
Type
protein
Length
630 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein LP_3323
UniProt
Q88SR8
Ligands
NA, MG, SO4
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative uncharacterized protein LP_3323protein21339% helix, 13% strandQ88SR8
BPutative uncharacterized protein LP_3323protein20938% helix, 13% strandQ88SR8
CPutative uncharacterized protein LP_3323protein20838% helix, 13% strandQ88SR8

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains B, A, C
  • MG · Magnesium ion · metal · chains B
  • SO4 · Sulfate ion · ion · 3 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110950.780.8072SO4, NA
2860.580.8724empty
31320.520.8125empty
41230.500.8020empty
51750.480.7622empty

Interfaces

3 interfaces between chains.

  • A–B · 885 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 866 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 812 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 3DC7 · Crystal structure of the protein Q88SR8 from Lactobacillus plantarum. Northeast… · the same entry in another collection · chain A against A, TM-score 1.00

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