Research workbench
Crystal structure of methyltransferase comt-S in P. praeruptorum
Analyse Crystal structure of methyltransferase comt-S in P. praeruptorum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IWT
- Type
- protein
- Length
- 692 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pmethyltransferase pcomt-S
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pmethyltransferase pcomt-S | protein | 346 | 49% helix, 16% strand | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.77 | 0.80 | 63 | empty |
| 2 | 872 | 0.76 | 0.79 | 73 | PEG |
| 3 | 219 | 0.58 | 0.79 | 24 | empty |
| 4 | 217 | 0.50 | 0.76 | 28 | empty |
| 5 | 188 | 0.46 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 4232 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 6IWT · Crystal structure of methyltransferase COMT-S in P. praeruptorum · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6IWT · PDBe 6IWT
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