Research workbench

Monolignol O-methyltransferase (momt)

Analyse Monolignol O-methyltransferase (momt) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3REO
Type: protein
Length: 1,421 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O04385

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	352	—	O04385
B	—	protein	353	—	O04385
C	—	protein	359	—	O04385
D	—	protein	357	—	O04385

Compared structures

3REO · Monolignol O-methyltransferase (MOMT) · the same entry in another collection · chain D against D, TM-score 1.00
O04385 · AlphaFold monomer V2.0 prediction for (ISO)EUGENOL O-methyltransferase (O04385) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O04385
Elsewhere: RCSB PDB 3REO · PDBe 3REO · UniProt O04385

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