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S. enterica hisa mutant D10G, DUP13-15,V14:2M, Q24L, G102

Analyse S. enterica hisa mutant D10G, DUP13-15,V14:2M, Q24L, G102 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5G1Y
Type
protein
Length
233 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
EC
5.3.1.16
UniProt
V7IJE3
Ligands
SO4
Pockets
1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A (EC 5.3.1.16)protein23342% helix, 24% strandV7IJE3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A
  • GOL · Glycerol · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15090.670.7844SO4

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

  • 5G1Y · S. enterica HisA mutant D10G, dup13-15,V14:2M, Q24L, G102 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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