MolNFT v1 · #53037 · protein
Structure of the histidine tagged, open cytochrome P450 eryk from S. erythraea
2WIO · Erythromycin B/D C-12 hydroxylase: “Structure of the histidine tagged, open cytochrome P450 eryk from S. erythraea”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.79). MolNFT v1 #53037 on GenesisL1: 3D structure…
- PDB
- 2WIO
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythromycin B/D C-12 hydroxylase
- EC
- 1.14.-.-
- UniProt
- P48635
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin B/D C-12 hydroxylase (EC 1.14.-.-) | protein | 393 | 53% helix, 10% strand | P48635 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 955 | 0.79 | 0.80 | 89 | HEM |
| 2 | 59 | 0.38 | 0.80 | 13 | empty |
Compared structures
- 2WIO · Structure of the histidine tagged, open cytochrome P450 Eryk from S. erythraea · 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 0.93
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 2WIO · PDBe 2WIO · UniProt P48635
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.