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Structural studies of N terminal deletion mutant of dps from mycobacterium smegmatis

Analyse Structural studies of N terminal deletion mutant of dps from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YW6
Type
protein
Length
448 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA protection during starvation protein
EC
1.16.-.-
UniProt
Q8VP75
Pockets
7 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA protection during starvation protein (EC 1.16.-.-)protein14877% helix, 3% strandQ8VP75
B, CDNA protection during starvation protein (EC 1.16.-.-)protein15077% helix, 3% strandQ8VP75

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14720.660.7847empty
21370.610.8515empty
3840.450.8017empty
41700.450.7526empty
51440.410.7422empty

Interfaces

3 interfaces between chains.

  • A–B · 446 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 445 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 444 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2YW6 · Structural studies of N terminal deletion mutant of Dps from Mycobacterium smegmatis · the same entry in another collection · chain A against A, TM-score 1.00

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