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Spcomt apo structure
Analyse Spcomt apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZY5
- Type
- protein
- Length
- 481 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable catechol O-methyltransferase 1
- EC
- 2.1.1.6
- UniProt
- O42898
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable catechol O-methyltransferase 1 (EC 2.1.1.6) | protein | 241 | 46% helix, 19% strand | O42898 |
| B | Probable catechol O-methyltransferase 1 (EC 2.1.1.6) | protein | 240 | 48% helix, 19% strand | O42898 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.49 | 0.78 | 29 | empty |
| 2 | 101 | 0.45 | 0.79 | 19 | empty |
| 3 | 125 | 0.40 | 0.75 | 24 | empty |
| 4 | 75 | 0.37 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 297 Ų buried · 2 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 O42898
- Elsewhere: RCSB PDB 5ZY5 · PDBe 5ZY5 · UniProt O42898
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