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Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily

Analyse Crystal structure of barley agmatine coumaroyltransferase (HvACT), an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CYS
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.81
Source: Hordeum vulgare
Molecule: Agmatine coumaroyltransferase-1
EC: 2.3.1.64
UniProt: A9ZPJ6
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · resolution 1.81 · 1 distinct chain · 29% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Agmatine coumaroyltransferase-1 (EC 2.3.1.64)	protein	431	29% helix, 25% strand	A9ZPJ6

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	698	0.78	0.83	91	empty
2	214	0.48	0.74	33	empty
3	72	0.37	0.77	14	empty

Modifications

Observed in the structure: 8 modified (artifact).

Compared structures

7CYS · Crystal structure of barley agmatine coumaroyltransferase (hvact), an N-acyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
A9ZPJ6 · AlphaFold monomer V2.0 prediction for agmatine coumaroyltransferase-1 (A9ZPJ6) · 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 A9ZPJ6
Elsewhere: RCSB PDB 7CYS · PDBe 7CYS · UniProt A9ZPJ6

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