Research workbench
Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidinoacetate
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
- 1XCJ
- 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, NMG
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanidinoacetate N-methyltransferase (EC 2.1.1.2) | protein | 229 | 38% helix, 26% strand | P10868 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.75 | 0.94 | 36 | SAH |
Compared structures
- 1XCJ · Guanidinoacetate methyltransferase containing S-adenosylhomocysteine and guanidinoacetate · 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 1XCJ · PDBe 1XCJ · UniProt P10868
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