Research workbench
Humanized rat comt in complex with 8-hydroxy-6-[3-methyl-5-(4- methylpiperazine-1-CARBONYL)THIOPHEN-2-yl]-3H-quinazolin-4-one
Analyse Humanized rat comt in complex with 8-hydroxy-6-[3-methyl-5-(4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5P9S
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22734
- Ligands
- 7JK, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 215 | — | P22734 |
Ligands and binding sites
- 7JK · 6-[3-methyl-5-(4-methylpiperazin-1-yl)carbonyl-thiophen-2-yl]-8-oxidanyl-3~{H}-quinazolin-4-one · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · 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 P22734
- Elsewhere: RCSB PDB 5P9S · PDBe 5P9S · UniProt P22734
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