Research workbench
Crystal structure of (S)-norcoclaurine 6-O-methyltransferase with S- adenosyl-L-homocysteine
Analyse Crystal structure of (S)-norcoclaurine 6-O-methyltransferase with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ICC
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5C9L7
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 353 | — | Q5C9L7 |
Compared structures
- Q5C9L7 · AlphaFold monomer V2.0 prediction for (rs)-norcoclaurine 6-O-methyltransferase (Q5C9L7) · 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 Q5C9L7
- Elsewhere: RCSB PDB 5ICC · PDBe 5ICC · UniProt Q5C9L7
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