Structure of PDB 1blz Chain A

Receptor sequence

>1blzA (length=327) Species: 162425 (Aspergillus nidulans)

SKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQRL
SQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESFC
YLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLSS
ALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTAA
DGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINCG
SYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPNG
KSDREPLSYGDYLQNGLVSLINKNGQT

3D structure

• PDB: 1blz Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.
• Chain: A
• Resolution: 1.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L186 F211 H214 D216 H270
• Catalytic site (residue number reindexed from 1): L182 F207 H210 D212 H266
• 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	FE	A	H214 D216 H270	H210 D212 H266
BS02	ACV	A	R87 S183 I187 Y189 H214 D216 S281 F285	R83 S179 I183 Y185 H210 D212 S277 F281
BS03	NO	A	H214 H270	H210 H266

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:1blz, PDBe:1blz, PDBj:1blz
• PDBsum: 1blz
• PubMed: 9194566
• UniProt: P05326|IPNA_EMENI Isopenicillin N synthase (Gene Name=ipnA)