Structure of PDB 5eqc Chain A Binding Site BS01

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 IDGLC
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-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain5eqc 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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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)		R63 E419 D423
Binding residue
(residue number reindexed from 1)		R48 E404 D408
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

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5eqc, PDBe:5eqc, PDBj:5eqc
PDBsum5eqc
PubMed
UniProtS8EY38

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