Structure of PDB 4ppm Chain B

Receptor sequence

>4ppmB (length=462) Species: 1327989 (Serratia sp. FS14)

ALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRS
AAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQ
YISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKP
GIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREA
LNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTG
LGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTA
DRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEI
AARYPFVSEVRGRGLMLGIQFDWHTTWKFLPDPVQAHLRAAMDRMEQALG
EMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFA
TVCEELSTFLDL

3D structure

• PDB: 4ppm Crystal structure of the catalytic domain of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M406 Y530 E583 D616 Q619 K645 T680 R822
• Catalytic site (residue number reindexed from 1): M35 Y159 E212 D245 Q248 K274 T309 R430
• Enzyme Commision number: 2.6.1.-

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	MG	B	A722 Y725 V728	A351 Y354 V357
BS02	PLP	B	G503 T504 Y530 H531 G532 D616 V618 K645	G132 T133 Y159 H160 G161 D245 V247 K274

Gene Ontology

Molecular Function

• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0042802 identical protein binding
• GO:0070280 pyridoxal binding

Biological Process

• GO:0017000 antibiotic biosynthetic process

External links

• PDB: RCSB:4ppm, PDBe:4ppm, PDBj:4ppm
• PDBsum: 4ppm
• PubMed: 24704447
• UniProt: A0A0J9X1Q5|PIGE_SERSF Aminotransferase PigE (Gene Name=pigE)