Structure of PDB 5zw7 Chain A

Receptor sequence

>5zw7A (length=383) Species: 104623 (Prodigiosinella confusarubida)

MDFNLSNSQSDIYESAYRFACDVLDQDAQTRISQKILSTELWKKAAAYGF
AHGPVSHQFGGSELGALDTALMIEALGKGSRDIGLSFSLCAHLCACVIPL
YRFGSSELKDKYLESLVTGKLIAANAATEPDAGSDIYNMQATAQPCEGGY
ILNGKKIFITNAPIADVFIIYAKTNPDHGFLGVSAFLIEKGTPGLNVGEV
IPKDCLSNCPWSEIVFNDIFIPQSQRIGMEGAGGAIFHDSMIWEKGCLSA
LFVGGLARLLETTLEYAKARQQFGKAIGQFQSVSNRIIDMKLRLEQCRLM
LYRACWKHDQGQDAEADIAMSKLLISEYAVQSGLDAIQTFGGAAMDQELG
LVRHLLNMIPSRIFSGTNDIQKEIIARKLGLRG

3D structure

• PDB: 5zw7 Crystal Structure of PigA: A Prolyl Thioester-Oxidizing Enzyme in Prodigiosin Biosynthesis.
• Chain: A
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A127 T128 E244 R377
• Catalytic site (residue number reindexed from 1): A127 T128 E244 R377
• Enzyme Commision number: 1.3.8.14: L-prolyl-[peptidyl-carrier protein] dehydrogenase.

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	A	N125 A127 T128 G133 S134 F158 I159 T160 W211 I363 T367 D369 I370	N125 A127 T128 G133 S134 F158 I159 T160 W211 I363 T367 D369 I370
BS02	O4B	A	E40 L41 K44	E40 L41 K44

Gene Ontology

Molecular Function

• 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

Biological Process

• GO:0017000 antibiotic biosynthetic process

External links

• PDB: RCSB:5zw7, PDBe:5zw7, PDBj:5zw7
• PDBsum: 5zw7
• PubMed: 30095206
• UniProt: Q5W271|PIGA_SERS3 L-prolyl-[peptidyl-carrier protein] dehydrogenase (Gene Name=pigA)