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Crystal structure of double mutant phenylalanine ammonia-lyase from anabaena variabilis

Analyse Crystal structure of double mutant phenylalanine ammonia-lyase from anabaena… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CZO
Type
protein
Length
2,150 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histidine ammonia-lyase
EC
4.3.1.3
UniProt
Q3M5Z3
Pockets
20 · best druggability 0.72

Structure

x-ray diffraction · 3 distinct chains · 58% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CHistidine ammonia-lyase (EC 4.3.1.3)protein53757% helix, 7% strandQ3M5Z3
BHistidine ammonia-lyase (EC 4.3.1.3)protein53958% helix, 6% strandQ3M5Z3
DHistidine ammonia-lyase (EC 4.3.1.3)protein53758% helix, 6% strandQ3M5Z3

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.720.9823empty
27710.690.7678empty
3650.660.9415empty
4690.580.8916empty
53420.580.7640empty

Interfaces

4 interfaces between chains.

  • A–B · 4406 Ų buried · 60 hydrogen bonds · protein-protein
  • A–C · 455 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 418 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 305 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 64 modified (engineered, nonstandard).

Compared structures

  • Q3M5Z3 · AlphaFold monomer V2.0 prediction for phenylalanine ammonia-lyase (Q3M5Z3) · a predicted model of the same protein · chain A against A, TM-score 1.00
  • 3CZO · Crystal Structure of Double Mutant Phenylalanine Ammonia-Lyase From Anabaena Variabilis · the same entry in another collection · chain B against B, TM-score 1.00

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