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Apo structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34H

Analyse Apo 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
2V28
Type
protein
Length
525 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine-4-hydroxylase
EC
1.14.16.1
UniProt
Q47XN7
Ligands
SO4
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine-4-hydroxylase (EC 1.14.16.1)protein26451% helix, 11% strandQ47XN7
BPhenylalanine-4-hydroxylase (EC 1.14.16.1)protein26152% helix, 11% strandQ47XN7

Ligands and binding sites

  • 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15360.750.8243empty
25180.730.8142empty
33470.650.8038empty
4630.280.7316empty

Interfaces

1 interface between chains.

  • A–B · 955 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2V28 · Apo structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea… · the same entry in another collection · chain A against A, TM-score 1.00

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