Structure of PDB 5e3k Chain A Binding Site BS01

Receptor Information
>5e3k Chain A (length=422) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKTNIEAYRDGLKLKTEEDFFACDRQYVCQNYAPVPVVISKGKGARVWDI
NGNEYYDFLAGVSSLSQGHCHPRVIAALCRQAERLTLTLRAFGNDVTGPA
CRFMAEMFGYDRVLLMNTGAEAGESALKIARKWAYEVKEIPPDSAKVILC
NNNYWGRTITACSSSTTFDCYNNFGPFTPGFELIDYDDVGALEEALKDPN
VAAFFVEPIQGEGGVNVPKPGYLKRAHELCRSKNVLLIVDEIQTGLCRTG
RLLAADHDEVHPDILLLGKSLSAGVVPISAVMGRADVMDVLKPGTHGSTF
GGNPLACAVAVEALTVLKDEKLADRAERLGAQFRDCLRRELYGKVPWIKE
IRGRGLLNAVEVDSDAIDPNDVVMKLKENGILSKPTRGRVMRFIPPLVIT
DEEHRDATTRIIKSFLAVEEER
Ligand information
Ligand ID5JV
InChIInChI=1S/C13H17N2O7P/c1-8(3-4-12(16)17)14-6-11-10(7-22-23(19,20)21)5-15-9(2)13(11)18/h5-6,18H,1,3-4,7H2,2H3,(H,16,17)(H2,19,20,21)/b14-6+
InChIKeyHRCALJQKZAULQS-MKMNVTDBSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1ncc(CO[P](O)(O)=O)c(C=NC(=C)CCC(O)=O)c1O
OpenEye OEToolkits 1.9.2Cc1c(c(c(cn1)COP(=O)(O)O)C=NC(=C)CCC(=O)O)O
OpenEye OEToolkits 1.9.2Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C(=C)CCC(=O)O)O
ACDLabs 12.01O=C(O)CC/C(N=C\c1c(cnc(c1O)C)COP(O)(O)=O)=C
FormulaC13 H17 N2 O7 P
Name4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid
ChEMBL
DrugBank
ZINCZINC000584904782
PDB chain5e3k Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5e3k Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with (S)-4-amino-5-fluoropentanoic acid
Resolution1.7 Å
Binding residue
(original residue number in PDB)		Y49 V79 G136 A137 Y171 W172 E229 D257 I259 Q260 K286
Binding residue
(residue number reindexed from 1)		Y32 V62 G119 A120 Y154 W155 E212 D240 I242 Q243 K269
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y171 E224 D257 Q260 K286 T316 R409
Catalytic site (residue number reindexed from 1) Y154 E207 D240 Q243 K269 T299 R392
Enzyme Commision number 2.6.1.13: ornithine aminotransferase.
Gene Ontology
Molecular Function
GO:0004587 ornithine aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0010121 arginine catabolic process to proline via ornithine
GO:0019544 arginine catabolic process to glutamate
GO:0055129 L-proline biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5e3k, PDBe:5e3k, PDBj:5e3k
PDBsum5e3k
PubMed
UniProtS8EY38

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