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Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidine

Analyse Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XCL
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanidinoacetate N-methyltransferase
EC: 2.1.1.2
UniProt: P10868
Ligands: SAH, GAI
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanidinoacetate N-methyltransferase (EC 2.1.1.2)	protein	229	36% helix, 28% strand	P10868

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
GAI · Guanidine · ligand · 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	123	0.77	0.96	37	SAH

Compared structures

1XCL · Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidine · the same entry in another collection · chain A against A, TM-score 1.00
P10868 · AlphaFold monomer V2.0 prediction for guanidinoacetate N-methyltransferase (P10868) · 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 P10868
Elsewhere: RCSB PDB 1XCL · PDBe 1XCL · UniProt P10868

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