MolNFT v1 · #12771 · protein
Crystal structure of human L-isoaspartyl methyltransferase
1KR5 · Protein-L-isoaspartate O-methyltransferase: “Crystal structure of human L-isoaspartyl methyltransferase”. X-ray diffraction, 1 ligand (SAH), 1 pocket (best druggability 0.71). MolNFT v1 #12771 on GenesisL1: 3D structure, binding…
- PDB
- 1KR5
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-L-isoaspartate O-methyltransferase
- EC
- 2.1.1.77
- UniProt
- P22061
- Ligands
- SAH
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-L-isoaspartate O-methyltransferase (EC 2.1.1.77) | protein | 218 | 35% helix, 26% strand | P22061 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.71 | 0.89 | 39 | SAH |
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 P22061
- Elsewhere: RCSB PDB 1KR5 · PDBe 1KR5 · UniProt P22061
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