MolNFT v1 · #74869 · protein

Crystal structure of perennial ryegrass LPOMT1 bound to sah

3P9C · Caffeic acid O-methyltransferase: “Crystal structure of perennial ryegrass LPOMT1 bound to sah”. X-ray diffraction, 2 ligands (SAH, DTV), 2 pockets (best druggability 0.76). MolNFT v1 #74869 on GenesisL1: 3D structure, binding sites…

PDB: 3P9C
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caffeic acid O-methyltransferase
EC: 2.1.1.6
UniProt: Q9ZTU2
Ligands: SAH, DTV
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Caffeic acid O-methyltransferase (EC 2.1.1.6)	protein	352	49% helix, 17% strand	Q9ZTU2

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
DTV · (2S,3S)-1,4-dimercaptobutane-2,3-diol · ligand · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

2 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	1015	0.76	0.78	70	SAH, ACT
2	61	0.38	0.79	15	empty

Compared structures

3P9C · Crystal structure of perennial ryegrass LpOMT1 bound to SAH · the same entry in another collection · 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 Q9ZTU2
Elsewhere: RCSB PDB 3P9C · PDBe 3P9C · UniProt Q9ZTU2

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