Structure of PDB 1odn Chain A

Receptor sequence
>1odnA (length=321) Species: 227321 (Aspergillus nidulans FGSC A4) [Search protein sequence]
SVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQ
RLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVES
FCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGL
SSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKT
AADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLIN
CGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREP
NGKSDREPLSYGDYLQNGLVS
3D structure
PDB1odn Crystallographic Studies on the Reaction of Isopenicillin N Synthase with an Unsaturated Substrate Analogue
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 APV A R87 S183 I187 Y189 H214 H270 S281 F285 R85 S181 I185 Y187 H212 H268 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1odn, PDBe:1odn, PDBj:1odn
PDBsum1odn
PubMed12926272
UniProtP05326|IPNA_EMENI Isopenicillin N synthase (Gene Name=ipnA)

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