Structure of PDB 4uoy Chain A

Receptor sequence

>4uoyA (length=454) Species: 562 (Escherichia coli)

SASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKS
VTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSA
VQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEA
ALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPG
FRHVPFGNIEAMRTALNECKKTGDDVAAVILEPIQGEGGVILPPPGYLTA
VRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGV
MPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLP
AQAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFAS
EMFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSV
EEAL

3D structure

• PDB: 4uoy Structure of Putrescine Aminotransferase from Escherichia Coli Provides Insights Into the Substrate Specificity Among Class III Aminotransferases.
• Chain: A
• Resolution: 2.305 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F50 F180 E238 D271 Q274 K300 T332 R426
• Catalytic site (residue number reindexed from 1): F44 F174 E232 D265 Q268 K294 T326 R420
• Enzyme Commision number: 2.6.1.29: diamine transaminase.
  2.6.1.82: putrescine--2-oxoglutarate transaminase.

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	PLP	A	G150 T151 F180 H181 G182 E238 D271 V273 Q274 K300	G144 T145 F174 H175 G176 E232 D265 V267 Q268 K294

Gene Ontology

Molecular Function

• GO:0008483 transaminase activity
• GO:0019161 diamine transaminase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0033094 putrescine--2-oxoglutarate transaminase activity
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0009447 putrescine catabolic process
• GO:0019477 L-lysine catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4uoy, PDBe:4uoy, PDBj:4uoy
• PDBsum: 4uoy
• PubMed: 25423189
• UniProt: P42588|PAT_ECOLI Putrescine aminotransferase (Gene Name=patA)