Research workbench
Structure of a mutant of P450 eryk in complex with erythromycin B.
Analyse Structure of a mutant of P450 eryk in complex with erythromycin B. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZKP
- Type
- protein
- Length
- 391 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythromycin C-12 hydroxylase
- EC
- 1.14.13.154
- UniProt
- P48635
- Ligands
- HEM, ERB
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin C-12 hydroxylase (EC 1.14.13.154) | protein | 391 | 53% helix, 11% strand | P48635 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.85 | 0.85 | 86 | HEM, ERB |
| 2 | 128 | 0.52 | 0.81 | 18 | empty |
| 3 | 82 | 0.36 | 0.76 | 20 | empty |
Compared structures
- 3ZKP · Structure of a mutant of P450 EryK in complex with erythromycin B. · 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 3ZKP · PDBe 3ZKP · UniProt P48635
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