Structure of PDB 4irn Chain G

Receptor sequence
>4irnG (length=378) Species: 272129 (Kamptonema sp. PCC 6506) [Search protein sequence]
AWNSQQIQFRKKVIQFAQQSLISDLIKNDKEEIFNRDAWQKCSEFGVHGW
PIPARYGGQELDILTTAYALQGLGYGCKDNGLIFAMNAHIWACEMPLLTF
GTEEQKEKYLPLLCRGGWIASHAATEPQAGSDIYSLKTTAQKDGDKYILN
GYKHYVTNGTIADLFIIFATIDPSLGKEGLTTFMIEKDTPGLILSKPISK
MGMRTAEVPELRLENCEVSAANRLGEEGTGLAIFNHSMEWERGFILAAAV
GTMERLLEQSIRYARSHKQFGQAIGKFQLVANKLVEMKLRLENAKAYLYK
VAWMKENKQMALLEASMANLYISEAWVQSCLEAIEIHGAYGYLTNTELER
ELRDAIASKFYSGTSEIQRVVIAKFLGL
3D structure
PDB4irn Structure of the prolyl-acyl carrier protein oxidase involved in the biosynthesis of the cyanotoxin anatoxin-a.
ChainG
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A127 T128 E244 S365 K377
Catalytic site (residue number reindexed from 1) A124 T125 E241 S362 K374
Enzyme Commision number 1.3.99.-
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 FAD G H125 A127 T128 S134 Y158 T160 F363 T367 E369 H122 A124 T125 S131 Y155 T157 F360 T364 E366
BS02 FAD G H270 F273 I277 F280 V283 E338 I339 G341 A342 H267 F270 I274 F277 V280 E335 I336 G338 A339
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:4irn, PDBe:4irn, PDBj:4irn
PDBsum4irn
PubMed24311576
UniProtC4NCB7

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