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Crystal structure of a member of the lipolytic protein G-D-S-L family from veillonella parvula dsm 2008

Analyse Crystal structure of a member of the lipolytic protein G-D-S-L family from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RW0
Type
protein
Length
367 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipolytic protein G-D-S-L family
UniProt
D1BPP2
Ligands
NA
Pockets
3 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALipolytic protein G-D-S-L familyprotein18448% helix, 15% strandD1BPP2
BLipolytic protein G-D-S-L familyprotein18348% helix, 15% strandD1BPP2

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1950.490.8115empty
21190.430.7720GOL
3810.400.7819empty

Interfaces

1 interface between chains.

  • A–B · 531 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 4RW0 · Crystal structure of a member of the lipolytic protein G-D-S-L family from Veillonella… · the same entry in another collection · chain A against A, TM-score 1.00

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