Research workbench
Isopenicillin N synthase C-terminal truncation mutant
Analyse Isopenicillin N synthase C-terminal truncation mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJS
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isopenicillin N synthetase
- EC
- 1.21.3.1
- UniProt
- P05326
- Ligands
- ACV, MEE, FE, SO4
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopenicillin N synthetase (EC 1.21.3.1) | protein | 320 | 29% helix, 21% strand | P05326 |
Ligands and binding sites
- ACV · L-D-(A-aminoadipoyl)-L-cysteinyl-D-valine · ligand · 2 copies · chains A
- MEE · Methanethiol · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 550 | 0.71 | 0.79 | 53 | FE, ACV |
Compared structures
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 P05326
- Elsewhere: RCSB PDB 2BJS · PDBe 2BJS · UniProt P05326
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