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Crystal structure of escherichia COLI phytase at pH 5.0 with HG2+ cation acting as an intermolecular bridge

Analyse Crystal structure of escherichia COLI phytase at pH 5.0 with HG2+ cation acting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DKN
Type
protein
Length
410 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phytase
EC
3.1.3.2
UniProt
P07102
Ligands
HG
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhytase (EC 3.1.3.2)protein41041% helix, 16% strandP07102

Ligands and binding sites

  • HG · Mercury (II) ion · metal · 5 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13990.610.7738empty
2570.330.7614empty
3700.310.7518empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1DKN · Crystal structure of escherichia COLI phytase at pH 5.0 with HG2+ cation acting as an… · the same entry in another collection · chain A against A, TM-score 1.00
  • P07102 · AlphaFold monomer V2.0 prediction for periplasmic appa protein (P07102) · a predicted model of the same protein · chain A against A, TM-score 1.00

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