Research workbench
Crystal structure of a carnosine N-methyltransferase bound by adohcy
Analyse Crystal structure of a carnosine N-methyltransferase bound by adohcy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5X62
- Type
- protein
- Length
- 763 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carnosine N-methyltransferase
- EC
- 2.1.1.22
- UniProt
- P53934
- Ligands
- SAH, NA
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carnosine N-methyltransferase (EC 2.1.1.22) | protein | 376 | 44% helix, 20% strand | P53934 |
| B | Carnosine N-methyltransferase (EC 2.1.1.22) | protein | 387 | 43% helix, 20% strand | P53934 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.75 | 0.78 | 94 | SAH |
| 2 | 842 | 0.74 | 0.78 | 88 | SAH |
| 3 | 109 | 0.55 | 0.84 | 29 | empty |
| 4 | 61 | 0.53 | 0.87 | 20 | empty |
| 5 | 60 | 0.49 | 0.86 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2907 Ų buried · 57 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5X62 · Crystal structure of a carnosine N-methyltransferase bound by AdoHcy · the same entry in another collection · chain A against A, TM-score 1.00
- P53934 · AlphaFold monomer V2.0 prediction for carnosine N-methyltransferase (P53934) · 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 P53934
- Elsewhere: RCSB PDB 5X62 · PDBe 5X62 · UniProt P53934
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