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Crystal structure of methyl transferase from methanosarcina mazei

Analyse Crystal structure of methyl transferase from methanosarcina mazei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MGG
Type
protein
Length
499 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methyltransferase
EC
2.1.1.-
UniProt
Q8PVL4
Pockets
5 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethyltransferase (EC 2.1.1.-)protein24646% helix, 25% strandQ8PVL4
BMethyltransferase (EC 2.1.1.-)protein25345% helix, 25% strandQ8PVL4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14590.660.7848empty
23170.590.7730empty
31600.470.7632empty
4980.390.7619empty
5500.250.7215empty

Interfaces

1 interface between chains.

  • A–B · 1153 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 3MGG · Crystal Structure of Methyl Transferase from Methanosarcina mazei · the same entry in another collection · chain A against A, TM-score 1.00

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