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Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34H

Analyse Structure of the cold active phenylalanine hydroxylase from colwellia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V27
Type
protein
Length
536 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine hydroxylase
EC
1.14.16.1
UniProt
Q47XN7
Ligands
FE, SO4
Pockets
6 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine hydroxylase (EC 1.14.16.1)protein26452% helix, 11% strandQ47XN7
BPhenylalanine hydroxylase (EC 1.14.16.1)protein27251% helix, 10% strandQ47XN7

Ligands and binding sites

  • FE · Fe (III) ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13250.790.9045empty
25120.740.8241empty
33330.660.8131empty
41500.450.7517empty
51180.350.7318empty

Interfaces

1 interface between chains.

  • A–B · 930 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2V27 · Structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H · the same entry in another collection · chain A against A, TM-score 1.00

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