Acc deaminase mutant complexed with acc

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Ligands and binding sites

• 5PA · N-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-Y-lmethyl]-1-amino-cyclopropanecarboxylic acid · ligand · 4 copies · chains A, B, C, D

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

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1999 Ų buried · 28 hydrogen bonds · protein-protein
• C–D · 1946 Ų buried · 23 hydrogen bonds · protein-protein
• B–D · 422 Ų buried · 4 hydrogen bonds · protein-protein
• A–D · 271 Ų buried · 3 hydrogen bonds · protein-protein
• B–C · 230 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 1J0D · ACC deaminase mutant complexed with ACC · the same entry in another collection · chain D against D, TM-score 1.00
• Q7M523 · AlphaFold monomer V2.0 prediction for 1-aminocyclopropane-1-carboxylate deaminase (Q7M523) · a predicted model of the same protein · chain C against A, TM-score 1.00

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 Q7M523
• Elsewhere: RCSB PDB 1J0D · PDBe 1J0D · UniProt Q7M523