Research workbench
Structure of cytochrome P450 eryk in complex with its natural substrate erd
Analyse Structure of cytochrome P450 eryk in complex with its natural substrate erd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JJO
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48635
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 393 | — | P48635 |
Compared structures
- 2JJO · Structure of cytochrome P450 EryK in complex with its natural substrate erD · the same entry in another collection · chain A against A, TM-score 1.00
- P48635 · AlphaFold monomer V2.0 prediction for erythromycin C-12 hydroxylase (P48635) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P48635
- Elsewhere: RCSB PDB 2JJO · PDBe 2JJO · UniProt P48635
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