MolNFT v2 · #118578 · protein
Structure of P450 StaH from glycopeptide antibiotic A47934 biosynthesis
5EX6: “Structure of P450 StaH from glycopeptide antibiotic A47934 biosynthesis”. X-ray diffraction at 2.4, 1 ligand (HEM). MolNFT v2 #118578 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5EX6
- Type
- protein
- Length
- 1,145 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Streptomyces toyocaensis
- UniProt
- Q8KLL9
- Ligands
- HEM
Structure
x-ray diffraction · resolution 2.4 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 388 | — | Q8KLL9 |
| A | — | protein | 386 | — | Q8KLL9 |
| B | — | protein | 371 | — | Q8KLL9 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains C, A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains C, A
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5EX6 · Structure of P450 stah from glycopeptide antibiotic A47934 biosynthesis · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8KLL9
- Elsewhere: RCSB PDB 5EX6 · PDBe 5EX6 · UniProt Q8KLL9
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