Complex of wild type E. COLI alpha aspartate decarboxylase with its processing factor panz

Structure

x-ray diffraction · 3 distinct chains · 22% helix, 42% strand (DSSP).

Ligands and binding sites

• PVO · 2,2-bis(oxidanyl)propanoic acid · ligand · chains A, D
• ACO · Acetyl coenzyme *A · ligand · chains B, D
• MG · Magnesium ion · metal · chains B
• CO2 · Carbon dioxide · ion · 3 copies · chains B, D
• SCN · Thiocyanate ion · ion · 2 copies · chains A, D, B
• 74C · methyl radical · ion · chains D
• GOL · Glycerol · additive · 2 copies · chains B, D
• PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains B, A, D

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–D · 1762 Ų buried · 42 hydrogen bonds · protein-protein
• B–D · 661 Ų buried · 5 hydrogen bonds · protein-protein
• A–B · 37 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 disulfide, 1 modified (covalent ligand, disulfide, oxidation).

Compared structures

• 5LS7 · Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ · the same entry in another collection · chain A against A, TM-score 1.00
• P0A790 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (P0A790) · a predicted model of the same protein · chain D against A, TM-score 1.00
• P37613 · AlphaFold monomer V2.0 prediction for pand regulatory factor (P37613) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P0A790
• Every structure of UniProt P37613
• Elsewhere: RCSB PDB 5LS7 · PDBe 5LS7 · UniProt P0A790 · UniProt P37613