Structure of PDB 2ivj Chain A

Receptor sequence

>2ivjA (length=329) Species: 227321 (Aspergillus nidulans FGSC A4)

SVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQ
RLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVES
FCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGL
SSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKT
AADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLIN
CGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREP
NGKSDREPLSYGDYLQNGLVSLINKNGQT

3D structure

• PDB: 2ivj Interactions of Isopenicillin N Synthase with Cyclopropyl-Containing Substrate Analogues Reveal New Mechanistic Insight.
• Chain: A
• Resolution: 1.46 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L186 F211 H214 D216 H270
• Catalytic site (residue number reindexed from 1): L184 F209 H212 D214 H268
• Enzyme Commision number: 1.21.3.1: isopenicillin-N synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	BCV	A	R87 C104 S183 I187 Y189 H214 D216 L223 S281 F285	R85 C102 S181 I185 Y187 H212 D214 L221 S279 F283
BS02	FE2	A	H214 D216 H270	H212 D214 H268

Gene Ontology

Molecular Function

• GO:0005506 iron ion binding
• GO:0016216 isopenicillin-N synthase activity
• GO:0016491 oxidoreductase activity
• GO:0031418 L-ascorbic acid binding
• GO:0046872 metal ion binding

Biological Process

• GO:0009058 biosynthetic process
• GO:0017000 antibiotic biosynthetic process
• GO:0042318 penicillin biosynthetic process
• GO:0044283 small molecule biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:2ivj, PDBe:2ivj, PDBj:2ivj
• PDBsum: 2ivj
• PubMed: 17397141
• UniProt: P05326|IPNA_EMENI Isopenicillin N synthase (Gene Name=ipnA)