MolNFT v1 · #17694 · protein
Guanidinoacetate methyltransferase with gd ion
1P1C · Guanidinoacetate N-methyltransferase: “Guanidinoacetate methyltransferase with gd ion”. X-ray diffraction, 2 ligands (SAH, GD3), 1 pocket (best druggability 0.81). MolNFT v1 #17694 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1P1C
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- 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, GD3
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Guanidinoacetate N-methyltransferase (EC 2.1.1.2) | protein | 193 | 39% helix, 27% strand | P10868 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- GD3 · Gadolinium ion · metal · chains A, B
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 | 572 | 0.81 | 0.86 | 84 | SAH |
Interfaces
1 interface between chains.
- A–B · 1223 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 1P1C · PDBe 1P1C · UniProt P10868
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