Structure of PDB 6zam Chain A

Receptor sequence
>6zamA (length=328) Species: 227321 (Aspergillus nidulans FGSC A4) [Search protein sequence]
VSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQR
LCQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESF
CYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLS
SALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTA
ADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINC
GSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPN
GKSDREPLSYGDYLQNGLVSLINKNGQT
3D structure
PDB6zam X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F211 H214 D216 H270
Catalytic site (residue number reindexed from 1) F208 H211 D213 H267
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 H211 D213 H267
BS02 W6X A Q52 C55 Q56 Q49 C52 Q53
BS03 W6Z A Q52 C55 Q56 Q49 C52 Q53
BS04 ACV A R87 S183 I187 Y189 H214 D216 S281 P283 F285 L324 R84 S180 I184 Y186 H211 D213 S278 P280 F282 L321
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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Biological Process
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Cellular Component
External links
PDB RCSB:6zam, PDBe:6zam, PDBj:6zam
PDBsum6zam
PubMed34417180
UniProtP05326|IPNA_EMENI Isopenicillin N synthase (Gene Name=ipnA)

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