Research workbench
Isopenicillin N synthase with substrate analogue ahcv
Analyse Isopenicillin N synthase with substrate analogue ahcv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZKU
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isopenicillin N synthase
- EC
- 1.21.3.1
- UniProt
- P05326
- Ligands
- HCV, FE
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopenicillin N synthase (EC 1.21.3.1) | protein | 325 | 30% helix, 21% strand | P05326 |
Ligands and binding sites
- HCV · N-[(5S)-5-amino-5-carboxypentanoyl]-L-homocysteyl-D-valine · ligand · chains A
- FE · Fe (III) ion · metal · 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 | 744 | 0.78 | 0.82 | 64 | FE, HCV |
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 3ZKU · PDBe 3ZKU · UniProt P05326
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