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The crystal structure of aspartate alpha-decarboxylase from campylobacter jejuni subsp. jejuni nctc 11168

Analyse The crystal structure of aspartate alpha-decarboxylase from campylobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PLX
Type
protein
Length
125 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aspartate 1-decarboxylase
EC
4.1.1.11
UniProt
Q9PIK3
Ligands
PYR

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAspartate 1-decarboxylase (EC 4.1.1.11)protein250% helix, 64% strandQ9PIK3
BAspartate 1-decarboxylase (EC 4.1.1.11)protein10022% helix, 43% strandQ9PIK3

Ligands and binding sites

  • PYR · Pyruvic acid · ligand · chains B
  • ACT · Acetate ion · additive · chains B
  • PEG · Di(hydroxyethyl)ether · additive · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 1723 Ų buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 3PLX · The crystal structure of aspartate alpha-decarboxylase from Campylobacter jejuni subsp.… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9PIK3 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (Q9PIK3) · a predicted model of the same protein · chain B against A, TM-score 0.95

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