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Crystal structure of phenylalanine hydroxylase from bacillus cereus atcc 14579

Analyse Crystal structure of phenylalanine hydroxylase from bacillus cereus atcc 14579 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VGM
Type
protein
Length
571 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine-4-hydroxylase
EC
1.14.16.1
UniProt
Q818B4
Ligands
FE
Pockets
5 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine-4-hydroxylase (EC 1.14.16.1)protein57145% helix, 19% strandQ818B4

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 7 copies · chains A
  • ACY · Acetic acid · additive · 3 copies · chains A
  • GOL · Glycerol · additive · 3 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110500.810.82103ACY
21200.460.7819empty
3780.320.7423empty
4640.300.7414PEG
5610.290.7414PEG

Compared structures

  • 7VGM · Crystal structure of Phenylalanine hydroxylase from Bacillus cereus ATCC 14579 · the same entry in another collection · chain A against A, TM-score 1.00

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