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●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

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Structure of PDB 4uoy Chain D Binding Site BS01

Receptor Information >4uoy Chain D (length=452) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] ASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSV TAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAV QNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAA LKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGF RHVPFGNIEAMRTALNECKKTGDDVAAVILEPIQGEGGVILPPPGYLTAV RKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVM PIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPA QAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASE MFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVE EA

Ligand information Ligand ID PLP InChI InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14) InChIKey NGVDGCNFYWLIFO-UHFFFAOYSA-N SMILES Software SMILES CACTVS 3.341 Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O OpenEye OEToolkits 1.5.0 Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O ACDLabs 10.04 O=P(O)(O)OCc1cnc(c(O)c1C=O)C Formula C8 H10 N O6 P Name PYRIDOXAL-5'-PHOSPHATE; VITAMIN B6 Phosphate ChEMBL CHEMBL82202 DrugBank DB00114 ZINC ZINC000001532514 PDB chain 4uoy Chain C Residue 800 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 4uoy Structure of Putrescine Aminotransferase from Escherichia Coli Provides Insights Into the Substrate Specificity Among Class III Aminotransferases. Resolution 2.305 Å Binding residue (original residue number in PDB) T331 T332 Binding residue (residue number reindexed from 1) T324 T325 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) F50 F180 E238 D271 Q274 K300 T332 R426 Catalytic site (residue number reindexed from 1) F43 F173 E231 D264 Q267 K293 T325 R419 Enzyme Commision number 2.6.1.29: diamine transaminase. 2.6.1.82: putrescine--2-oxoglutarate transaminase.

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

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