Research workbench

Isopenicillin N synthase from aspergillus nidulans (acv-fe complex)

Analyse Isopenicillin N synthase from aspergillus nidulans (acv-fe complex) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BK0
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isopenicillin N synthase
UniProt: P05326
Ligands: ACV, FE, SO4
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isopenicillin N synthase	protein	329	30% helix, 21% strand	P05326

Ligands and binding sites

ACV · L-D-(A-aminoadipoyl)-L-cysteinyl-D-valine · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	526	0.82	0.88	65	ACV

Compared structures

1BK0 · Isopenicillin N synthase from aspergillus nidulans (acv-fe complex) · the same entry in another collection · chain A against A, TM-score 1.00
P05326 · AlphaFold monomer V2.0 prediction for isopenicillin N synthase (P05326) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 1BK0 · PDBe 1BK0 · UniProt P05326

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