Structure of PDB 4uoy Chain D Binding Site BS02

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 IDPLP
InChIInChI=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)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain4uoy Chain D Residue 800 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4uoy Structure of Putrescine Aminotransferase from Escherichia Coli Provides Insights Into the Substrate Specificity Among Class III Aminotransferases.
Resolution2.305 Å
Binding residue
(original residue number in PDB)		S149 G150 T151 F180 H181 G182 D271 V273 K300
Binding residue
(residue number reindexed from 1)		S142 G143 T144 F173 H174 G175 D264 V266 K293
Annotation score1
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4uoy, PDBe:4uoy, PDBj:4uoy
PDBsum4uoy
PubMed25423189
UniProtP42588|PAT_ECOLI Putrescine aminotransferase (Gene Name=patA)

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