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Methyltransferase bound with methyltetrahydrofolate

Analyse Methyltransferase bound with methyltetrahydrofolate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YCJ
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase
UniProt: Q3ACR9
Ligands: C2F, SO4
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase	protein	271	50% helix, 15% strand	Q3ACR9

Ligands and binding sites

C2F · 5-methyl-5,6,7,8-tetrahydrofolic acid · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
GOL · Glycerol · additive · 3 copies · 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	304	0.55	0.76	37	GOL, C2F
2	75	0.45	0.82	25	empty

Compared structures

2YCJ · methyltransferase bound with methyltetrahydrofolate · 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 Q3ACR9
Elsewhere: RCSB PDB 2YCJ · PDBe 2YCJ · UniProt Q3ACR9

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