Structure of PDB 1oc1 Chain A

Receptor sequence

>1oc1A (length=329) Species: 227321 (Aspergillus nidulans FGSC A4)

SVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQ
RLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVES
FCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGL
SSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKT
AADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLIN
CGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREP
NGKSDREPLSYGDYLQNGLVSLINKNGQT

3D structure

• PDB: 1oc1 Structural Studies on the Reaction of Isopenicillin N Synthase with the Substrate Analogue Delta-(L-Alpha-Aminoadipoyl)-L-Cysteinyl-D-Alpha-Aminobutyrate
• Chain: A
• Resolution: 2.2 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	ASV	A	R87 C104 S183 Y189 F211 H214 D216 S281 P283 F285 T331	R85 C102 S181 Y187 F209 H212 D214 S279 P281 F283 T329
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:1oc1, PDBe:1oc1, PDBj:1oc1
• PDBsum: 1oc1
• PubMed: 12622704
• UniProt: P05326|IPNA_EMENI Isopenicillin N synthase (Gene Name=ipnA)