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Crystal structure of agmatine coumaroyltransferase from triticum aestivum

Analyse Crystal structure of agmatine coumaroyltransferase from triticum aestivum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DTP
Type
protein
Length
408 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Agmatine coumaroyltransferase
UniProt
A0A3B6DKZ2
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAgmatine coumaroyltransferaseprotein40828% helix, 25% strandA0A3B6DKZ2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17650.760.8172empty
2640.360.7713empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7DTP · Crystal structure of agmatine coumaroyltransferase from Triticum aestivum · the same entry in another collection · chain A against A, TM-score 1.00

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