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Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease

Analyse Accommodation of insertion mutations on the surface and in the interior of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1STA
Type
protein
Length
137 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Staphylococcal nuclease
EC
3.1.31.1
UniProt
P00644
Ligands
THP, CA
Pockets
1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStaphylococcal nuclease (EC 3.1.31.1)protein13726% helix, 31% strandP00644

Ligands and binding sites

  • THP · Thymidine-3',5'-diphosphate · ligand · chains A
  • CA · Calcium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.480.7828CA, THP

Compared structures

  • 1STA · Accommodation of insertion mutations on the surface and in the interior of staphylococcal… · the same entry in another collection · chain A against A, TM-score 1.00

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