Structure of PDB 5eqc Chain A Binding Site BS02

Receptor Information
>5eqc Chain A (length=426) Species: 5811 (Toxoplasma gondii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GARKTNIEAYRDGLKLKTEEDFFACDRQYVCQNYAPVPVVISKGKGARVW
DINGNEYYDFLAGVSSLSQGHCHPRVIAALCRQAERLTLTLRAFGNDVTG
PACRFMAEMFGYDRVLLMNTGAEAGESALKIARKWAYEVKEIPPDSAKVI
LCNNNYWGRTITACSSSTTFDCYNNFGPFTPGFELIDYDDVGALEEALKD
PNVAAFFVEPIQGEGGVNVPKPGYLKRAHELCRSKNVLLIVDEIQTGLCR
TGRLLAADHDEVHPDILLLGKSLSAGVVPISAVMGRADVMDVLKPGTHGS
TFGGNPLACAVAVEALTVLKDEKLADRAERLGAQFRDCLRRELYGKVPWI
KEIRGRGLLNAVEVDSDAIDPNDVVMKLKENGILSKPTRGRVMRFIPPLV
ITDEEHRDATTRIIKSFLAVEEERKK
Ligand information
Ligand IDBGC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChIKeyWQZGKKKJIJFFOK-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain5eqc Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5eqc Structure of the ornithine aminotransferase from Toxoplasma gondii crystallized in presence of oxidized glutathione reveals partial occupancy of PLP at the protein active site
Resolution2.2 Å
Binding residue
(original residue number in PDB)		R369 G370 R371
Binding residue
(residue number reindexed from 1)		R354 G355 R356
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) Y156 E209 D242 Q245 K271 T301 R394
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:5eqc, PDBe:5eqc, PDBj:5eqc
PDBsum5eqc
PubMed
UniProtS8EY38

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