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Crystal structure of glycine sarcosine N-methyltransferase from methanohalophilus portucalensis in complex with S- adenosylhomocysteine and sarcosine

Analyse Crystal structure of glycine sarcosine N-methyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HIL
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycine sarcosine N-methyltransferase
EC: 2.1.1.156
UniProt: F6KV61
Ligands: SAH, SAR
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycine sarcosine N-methyltransferase (EC 2.1.1.156)	protein	240	38% helix, 30% strand	F6KV61

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
SAR · Sarcosine · ligand · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	720	0.79	0.83	59	SAH, SAR, EDO

Compared structures

5HIL · Crystal structure of glycine sarcosine N-methyltransferase from Methanohalophilus… · 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 F6KV61
Elsewhere: RCSB PDB 5HIL · PDBe 5HIL · UniProt F6KV61

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