Research workbench

Arabidopsis thaliana prephenate aminotransferase double mutant- T84V K169V

Analyse Arabidopsis thaliana prephenate aminotransferase double mutant- T84V K169V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WMK
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional aspartate aminotransferase and GLUTAMATE/ASPARTATE-prephenate…
EC: 2.6.1.1, 2.6.1.78, 2.6.1.79
UniProt: Q9SIE1
Ligands: BO3
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional aspartate aminotransferase and GLUTAMATE/ASPARTATE-prephenate aminotransferase (EC 2.6.1.1, 2.6.1.78, 2.6.1.79)	protein	403	46% helix, 16% strand	Q9SIE1

Ligands and binding sites

BO3 · Boric acid · ion · chains A
MLI · Malonate ion · additive · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.63	0.80	51	MLI, BO3

Compared structures

5WMK · Arabidopsis thaliana Prephenate Aminotransferase double mutant- T84V K169V · the same entry in another collection · chain A against A, TM-score 1.00
Q9SIE1 · AlphaFold monomer V2.0 prediction for bifunctional aspartate aminotransferase and… · a predicted model of the same protein · chain A 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 Q9SIE1
Elsewhere: RCSB PDB 5WMK · PDBe 5WMK · UniProt Q9SIE1

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