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Phenylalanine ammonia-lyase (pal) from petroselinum crispum

Analyse Phenylalanine ammonia-lyase (pal) from petroselinum crispum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1W27
Type
protein
Length
1,380 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine ammonia-lyase 1
EC
4.3.1.5
UniProt
P24481
Pockets
18 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhenylalanine ammonia-lyase 1 (EC 4.3.1.5)protein69057% helix, 4% strandP24481

Ligands and binding sites

  • DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 2 copies · chains A, B

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

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12290.830.9631empty
24590.650.7860DTT
33820.620.7844DTT
43050.600.7840empty
52920.590.7736empty

Interfaces

1 interface between chains.

  • A–B · 4393 Ų buried · 64 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent, 2 modified (additive adduct, nonstandard).

Compared structures

  • 1W27 · Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum · the same entry in another collection · chain A against A, TM-score 1.00
  • P24481 · AlphaFold monomer V2.0 prediction for phenylalanine ammonia-lyase 1 (P24481) · a predicted model of the same protein · chain A against A, TM-score 0.97

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